Toolkit/Caenorhabditis elegans light-induced coclustering

Caenorhabditis elegans light-induced coclustering

Assay Method·Research·Since 2021

Also known as: CeLINC

Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

Caenorhabditis elegans light-induced coclustering (CeLINC) is a fluorescence-based optical binary protein-protein interaction assay for testing whether two proteins interact in vivo in C. elegans. It uses light-induced coclustering as the assay readout for protein association.

Usefulness & Problems

Why this is useful

CeLINC is useful for assessing binary protein association directly in the living C. elegans context rather than outside the organism. The reported applications show that it can distinguish positive interactions among apical polarity regulators from cases where no physical interaction was observed among basolateral Scribble module proteins.

Source:

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3

Source:

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

Source:

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.

Problem solved

CeLINC addresses the problem of determining whether two proteins physically interact in vivo in C. elegans using an optical assay. The available evidence does not provide further detail on sensitivity, temporal resolution, or quantitative performance.

Source:

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3

Source:

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

Problem links

Lack of Structure Prediction for Highly Dynamic Proteins

Gap mapView gap

For dynamic proteins, interaction readouts can sometimes provide indirect evidence about state-dependent behavior. CeLINC is an in vivo protein-protein interaction assay, so it could plausibly help probe allostery-linked interaction changes, though it does not address structure prediction directly.

Taxonomy & Function

Primary hierarchy

Technique Branch

Method: A concrete measurement method used to characterize an engineered system.

Target processes

localization

Input: Light

Implementation Constraints

cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensor

The assay is described as fluorescence-based, optical, and dependent on light-induced coclustering in C. elegans. The provided evidence does not specify the photoreceptor system, wavelengths, cofactors, expression strategy, or fusion construct design.

The supplied evidence is limited to a single 2021 report and a small number of example protein pairs in C. elegans. No details are provided here on false-positive or false-negative rates, illumination parameters, construct architecture, or validation outside the reported polarity regulators.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 2application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 3application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 4application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 5application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 6application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 7application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 8application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 9application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 10application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 11application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 12application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 13application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 14application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 15application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 16application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 17application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 18application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 19application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 20application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 21application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 22application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 23application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 24application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 25application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 26application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 27application resultsupports2021Source 1needs review

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3
Claim 28application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 29application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 30application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 31application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 32application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 33application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 34application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 35application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 36application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 37application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 38application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 39application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 40application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 41application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 42application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 43application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 44application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 45application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 46application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 47application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 48application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 49application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 50application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 51application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 52application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 53application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 54application resultsupports2021Source 1needs review

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.
Claim 55capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 56capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 57capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 58capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 59capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 60capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 61capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 62capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 63capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 64capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 65capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 66capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 67capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 68capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 69capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 70capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 71capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 72capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 73capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 74capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 75capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 76capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 77capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 78capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 79capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 80capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 81capabilitysupports2021Source 1needs review

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.
Claim 82mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 83mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 84mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 85mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 86mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 87mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 88mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 89mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 90mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 91mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 92mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 93mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 94mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 95mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 96mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 97mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 98mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 99mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 100mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 101mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 102mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 103mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 104mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 105mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 106mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 107mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 108mechanismsupports2021Source 1needs review

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.
Claim 109performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 110performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 111performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 112performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 113performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 114performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 115performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 116performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 117performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 118performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 119performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 120performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 121performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 122performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 123performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 124performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 125performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 126performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 127performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 128performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 129performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 130performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 131performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 132performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 133performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 134performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 135performancesupports2021Source 1needs review

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.
Claim 136usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 137usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 138usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 139usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 140usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 141usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 142usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 143usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 144usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 145usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 146usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 147usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 148usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 149usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 150usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 151usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 152usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 153usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 154usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 155usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 156usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 157usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 158usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 159usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 160usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 161usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.
Claim 162usabilitysupports2021Source 1needs review

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.

Approval Evidence

1 source6 linked approval claimsfirst-pass slug caenorhabditis-elegans-light-induced-coclustering
We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.

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application resultsupports

Using CeLINC, the authors confirmed interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3.

We confirmed interactions seen between PAR-6, PKC-3, and PAR-3

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application resultsupports

Using CeLINC, the authors observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

but observed no physical interactions among the basolateral Scribble module proteins LET-413, DLG-1, and LGL-1.

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capabilitysupports

CeLINC is an optical binary protein-protein interaction assay for determining whether two proteins interact in vivo in Caenorhabditis elegans.

We present Caenorhabditis elegans light-induced coclustering (CeLINC), an optical binary protein-protein interaction assay to determine whether two proteins interact in vivo.

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mechanismsupports

CeLINC is based on CRY2/CIB1 light-dependent oligomerization and detects interaction by colocalization of a fluorescently tagged prey protein with clustered bait protein.

Based on CRY2/CIB1 light-dependent oligomerization, CeLINC can rapidly and unambiguously identify protein-protein interactions between pairs of fluorescently tagged proteins. A fluorescently tagged bait protein is captured using a nanobody directed against the fluorescent protein (GFP or mCherry) and brought into artificial clusters within the cell. Colocalization of a fluorescently tagged prey protein in the cluster indicates a protein interaction.

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performancesupports

In the reported reference-pair testing, CeLINC showed extremely robust assay performance with no false positives detected in the negative reference pairs.

We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.

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usabilitysupports

The CeLINC plasmid toolkit allows use of custom promoters or CRY2 variants and supports use with existing fluorescently tagged strains without additional cloning or genome modification.

We have generated a plasmid toolkit that allows use of custom promoters or CRY2 variants to promote flexibility of the system. The CeLINC assay is a powerful and rapid technique that can be widely applied in C. elegans due to the universal plasmids that can be used with existing fluorescently tagged strains without need for additional cloning or genetic modification of the genome.

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Comparisons

Source-backed strengths

The method was reported to confirm interactions among the apical polarity regulators PAR-6, PKC-3, and PAR-3 in vivo. It also yielded negative results for LET-413, DLG-1, and LGL-1, indicating that the assay can support both detection of association and observation of no physical interaction in the tested polarity protein sets.

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We tested the system with an array of positive and negative reference protein pairs. Assay performance was extremely robust with no false positives detected in the negative reference pairs.

Compared with Cry2

Caenorhabditis elegans light-induced coclustering and Cry2 address a similar problem space because they share localization.

Shared frame: shared target processes: localization; shared mechanisms: oligomerization; same primary input modality: light

Strengths here: looks easier to implement in practice; may avoid an exogenous cofactor requirement.

Relative tradeoffs: appears more independently replicated.

Compared with IRAP-pHluorin translocation assay

Caenorhabditis elegans light-induced coclustering and IRAP-pHluorin translocation assay address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; same primary input modality: light

Compared with Iris

Caenorhabditis elegans light-induced coclustering and Iris address a similar problem space because they share localization.

Shared frame: same top-level item type; shared target processes: localization; same primary input modality: light

Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.

Ranked Citations

  1. 1.
    StructuralSource 1Genetics2021Claim 26Claim 26Claim 27

    Seeded from load plan for claim c3. Extracted from this source document.