Source 1primary paper2022
Toolkit/iLID-antiGFP-nanobody
iLID-antiGFP-nanobody
Also known as: antiGFP nanobody fused to iLID
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
iLID-antiGFP-nanobody is a multi-component optogenetic recruitment system in which iLID is fused to an antiGFP nanobody to target existing GFP-tagged proteins. Under blue-light illumination, iLID heterodimerizes with SspB, enabling light-dependent recruitment to locations defined by GFP fusions.
Usefulness & Problems
Why this is useful
This system is useful because it redirects iLID-based optogenetic recruitment to pre-existing GFP-tagged proteins rather than requiring direct engineering of each target protein. The reported advantage is increased targeting flexibility while retaining efficient light-dependent SspB recruitment.
Source:
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
Problem solved
It addresses the practical problem of deploying iLID recruitment at specific intracellular targets when those targets are already available as GFP fusions. The antiGFP nanobody-iLID fusion allows use of existing GFP-tagged proteins without modifying the iLID target itself.
Problem links
Need conditional recombination or state switching
DerivediLID-antiGFP-nanobody is a multi-component optogenetic recruitment system in which iLID is fused to an antiGFP nanobody to target GFP-tagged proteins. Upon blue-light illumination, iLID heterodimerizes with SspB, enabling light-dependent recruitment at sites defined by existing GFP fusions.
Need inducible protein relocalization or recruitment
DerivediLID-antiGFP-nanobody is a multi-component optogenetic recruitment system in which iLID is fused to an antiGFP nanobody to target GFP-tagged proteins. Upon blue-light illumination, iLID heterodimerizes with SspB, enabling light-dependent recruitment at sites defined by existing GFP fusions.
Need precise spatiotemporal control with light input
DerivediLID-antiGFP-nanobody is a multi-component optogenetic recruitment system in which iLID is fused to an antiGFP nanobody to target GFP-tagged proteins. Upon blue-light illumination, iLID heterodimerizes with SspB, enabling light-dependent recruitment at sites defined by existing GFP fusions.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
light-dependent protein recruitmentlight-dependent protein recruitmentlight-induced heterodimerizationlight-induced heterodimerizationnanobody-mediated targetingnanobody-mediated targetingTechniques
No technique tags yet.
Target processes
localizationrecombinationInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: multi componentswitch architecture: recruitment
The construct design supported by the evidence is a fusion of iLID to an antiGFP nanobody, used together with an SspB binding partner. Blue light is the activating input, and targeting depends on the presence of a GFP-tagged protein serving as the localization anchor.
The supplied evidence is limited to a single 2022 source and does not provide quantitative performance metrics, kinetic parameters, or validation across multiple proteins, organisms, or assay formats. No evidence here addresses background binding, reversibility, phototoxicity, or performance outside the reported context.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
recruitment efficiency still functioning efficiently
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
iLID and SspB heterodimerize upon blue-light illumination.
It comprises two components, iLID and SspB, which heterodimerize upon illumination with blue light.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug ilid-antigfp-nanobody
To skip the modification of the iLID and use existing GFP fusion as targets, we fuse an antiGFP nanobody to the iLID.
Source:
functional compatibilitysupports
Light-dependent recruitment of SspB remains efficient when iLID is localized to a GFP-tagged protein via an antiGFP nanobody.
the light-dependent recruitment of SspB to iLID, localized by the antiGFP nanobody to a GFP-tagged protein, is still functioning efficiently
Source:
practical advantagesupports
The iLID-antiGFP-nanobody approach increases flexibility by enabling recruitment to GFP-tagged proteins without requiring protein engineering of iLID targets.
This approach increases flexibility, enabling the recruitment of any GFP-tagged protein, without the necessity of protein engineering.
Source:
targeting functionsupports
An antiGFP nanobody fused to iLID can localize iLID to GFP-tagged proteins.
We show that the antiGFP nanobody is able to locate iLID to GFP-tagged proteins.
Source:
Comparisons
Source-backed strengths
Source claims indicate that SspB recruitment remains efficient when iLID is localized through an antiGFP nanobody to a GFP-tagged protein. The approach also expands experimental flexibility by leveraging established GFP fusion collections for light-controlled recruitment.
Compared with ArrayG
iLID-antiGFP-nanobody and ArrayG address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; same primary input modality: light
iLID-antiGFP-nanobody and CRY2-talin/CIBN-CAAX optogenetic plasma membrane recruitment system address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; shared mechanisms: light-induced heterodimerization; same primary input modality: light
Compared with PA-Cre2.0
iLID-antiGFP-nanobody and PA-Cre2.0 address a similar problem space because they share localization, recombination.
Shared frame: same top-level item type; shared target processes: localization, recombination; shared mechanisms: light-induced heterodimerization; same primary input modality: light
Ranked Citations
- 1.