Source 1primary paper2016Journal of Cell Science
Toolkit/IRAP-pHluorin translocation assay
IRAP-pHluorin translocation assay
Also known as: live-cell kinetic analyses of IRAP-pHluorin translocation
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The IRAP-pHluorin translocation assay is a live-cell kinetic imaging assay that monitors translocation of an IRAP/LNPEP-pHluorin reporter as a surrogate readout for GLUT4 trafficking in adipocytes. In the cited study, it was used to quantify stimulus-dependent membrane translocation responses downstream of optogenetic PI3K/PIP3 and Akt pathway activation.
Usefulness & Problems
Why this is useful
This assay is useful for real-time measurement of adipocyte membrane trafficking responses linked to insulin signaling, using IRAP/LNPEP as a surrogate marker for GLUT4 behavior. In the cited work, it enabled comparison of the extent of translocation induced by Opto-PIP3, Opto-Akt, insulin stimulation, and Akt inhibition.
Source:
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
Problem solved
It addresses the need for a live-cell, kinetic readout of GLUT4-associated trafficking that can be coupled to spatially and temporally controlled signaling perturbations. In the cited study, it helped distinguish the contributions of PI3K/PIP3 and Akt to adipocyte insulin action by reporting translocation outcomes downstream of optogenetic activation.
Problem links
Need conditional control of signaling activity
DerivedThe IRAP-pHluorin translocation assay is a live-cell kinetic imaging method that tracks translocation of IRAP/LNPEP, used here as a surrogate marker for GLUT4 trafficking in adipocytes. In the cited study, it was used to quantify stimulus-dependent membrane translocation and vesicle fusion responses downstream of optogenetic PI3K/PIP3 and Akt pathway activation.
Need inducible protein relocalization or recruitment
DerivedThe IRAP-pHluorin translocation assay is a live-cell kinetic imaging method that tracks translocation of IRAP/LNPEP, used here as a surrogate marker for GLUT4 trafficking in adipocytes. In the cited study, it was used to quantify stimulus-dependent membrane translocation and vesicle fusion responses downstream of optogenetic PI3K/PIP3 and Akt pathway activation.
Need precise spatiotemporal control with light input
DerivedThe IRAP-pHluorin translocation assay is a live-cell kinetic imaging method that tracks translocation of IRAP/LNPEP, used here as a surrogate marker for GLUT4 trafficking in adipocytes. In the cited study, it was used to quantify stimulus-dependent membrane translocation and vesicle fusion responses downstream of optogenetic PI3K/PIP3 and Akt pathway activation.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Mechanisms
fluorescence-based live-cell reporting of translocationfluorescence-based live-cell reporting of translocationspatially localized signaling perturbationspatially localized signaling perturbationvesicle fusion readoutvesicle fusion readoutTechniques
Functional AssayTarget processes
localizationsignalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: sensor
Implementation requires expression of an IRAP/LNPEP-pHluorin reporter and live-cell kinetic imaging. The cited application used the assay in adipocytes together with optogenetic PI3K/PIP3 and Akt pathway activation, but the supplied evidence does not specify construct architecture, imaging settings, or delivery method.
The readout is based on IRAP/LNPEP as a surrogate marker for GLUT4 rather than direct measurement of GLUT4 itself. The supplied evidence is limited to one study context in adipocytes and does not provide broader validation across cell types, perturbation classes, or independent replication.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
Drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3.
Conversely, drug-mediated inhibition of Akt only partially dampened the translocation response of Opto-PIP3
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
PI3K and Akt play distinct roles in adipocyte insulin action, and PI3K stimulates Akt-independent pathways important for GLUT4 translocation.
Taken together, these results indicate that PI3K and Akt play distinct roles, and that PI3K stimulates Akt-independent pathways that are important for GLUT4 translocation.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
The study describes optogenetic tools based on CRY2 and CIBN that selectively activate PI3K and Akt in time and space in 3T3-L1 adipocytes.
Here, we describe new optogenetic tools based on CRY2 and the N-terminus of CIB1 (CIBN). We used these 'Opto' modules to activate PI3K and Akt selectively in time and space in 3T3-L1 adipocytes.
Approval Evidence
1 source2 linked approval claimsfirst-pass slug irap-phluorin-translocation-assay
performed live-cell kinetic analyses of IRAP-pHluorin translocation (IRAP is also known as LNPEP and acts as a surrogate marker for GLUT4 here)
Source:
comparative effectsupports
Opto-PIP3 largely mimicked the maximal effects of insulin stimulation on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation.
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Source:
spatial localization effectsupports
Focal targeting of Akt to a region of the cell marked sites where IRAP-pHluorin vesicles fused, supporting local Akt-mediated regulation of exocytosis.
In spatial optogenetic studies, focal targeting of Akt to a region of the cell marked the sites where IRAP-pHluorin vesicles fused, supporting the idea that local Akt-mediated signaling regulates exocytosis.
Source:
Comparisons
Source-backed strengths
The assay provides live-cell kinetic analysis of IRAP-pHluorin translocation rather than endpoint measurement. In the cited study, it resolved differential pathway outputs, showing that Opto-PIP3 largely mimicked maximal insulin effects on IRAP-pHluorin translocation, whereas Opto-Akt only partially triggered translocation, and that Akt inhibition only partially dampened the Opto-PIP3 response.
Source:
Strikingly, Opto-PIP3 largely mimicked the maximal effects of insulin stimulation, whereas Opto-Akt only partially triggered translocation.
Compared with BcLOV4 photoreceptor
IRAP-pHluorin translocation assay and BcLOV4 photoreceptor address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; same primary input modality: light
Compared with fusion proteins with large N-terminal anchors
IRAP-pHluorin translocation assay and fusion proteins with large N-terminal anchors address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; same primary input modality: light
Strengths here: looks easier to implement in practice.
Compared with LOVpep/ePDZb
IRAP-pHluorin translocation assay and LOVpep/ePDZb address a similar problem space because they share localization, signaling.
Shared frame: shared target processes: localization, signaling; same primary input modality: light
Relative tradeoffs: appears more independently replicated.
Ranked Citations
- 1.