Toolkit/NIR Rac1 biosensor

NIR Rac1 biosensor

Construct Pattern·Research·Since 2018

Also known as: NIR biosensor for Rac1 GTPase, Rac1 biosensor

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

Summary

The NIR Rac1 biosensor is a near-infrared FRET construct engineered to report Rac1 GTPase activity. It was developed for multiplexed imaging of Rho GTPase signaling and was used to monitor Rac1 activity during optogenetic manipulation in the same cells.

Usefulness & Problems

Why this is useful

This biosensor is useful because it places Rac1 activity readout in a near-infrared channel, preserving visible spectral space for other fluorescent biosensors and blue-green optogenetic actuators. The reported application enabled simultaneous observation of Rac1 activity during light-based perturbation of Rho GTPase signaling pathways.

Source:

The NIR Rac1 biosensor reports Rac1 GTPase activity in a near-infrared imaging channel. The abstract states that it was used for multiplexed imaging and during optogenetic manipulation of Rac1.

Source:

monitoring Rac1 activity

Source:

multiplexed imaging of Rho GTPase signaling

Source:

simultaneous imaging during optogenetic manipulation

Problem solved

It addresses the experimental problem of monitoring Rac1 signaling while concurrently performing multiplex imaging and optogenetic control in the same cell. The cited work specifically positions it as a solution for observing Rac1 activity without consuming the spectral channels used by CFP-YFP biosensors and LOV-TRAP-based light control.

Source:

It solves the need to observe Rac1 activity while preserving spectral space for other fluorescent biosensors and blue-green optogenetic actuators.

Source:

enabling Rac1 activity imaging in a spectral window compatible with other biosensors and optogenetic tools

Problem links

enabling Rac1 activity imaging in a spectral window compatible with other biosensors and optogenetic tools

Literature

It solves the need to observe Rac1 activity while preserving spectral space for other fluorescent biosensors and blue-green optogenetic actuators.

Source:

It solves the need to observe Rac1 activity while preserving spectral space for other fluorescent biosensors and blue-green optogenetic actuators.

Published Workflows

Direct multiplex imaging and optogenetics of Rho GTPases enabled by near-infrared FRET

2018

Objective: Develop a near-infrared FRET-based Rac1 biosensor and use it together with visible-spectrum biosensors and optogenetic control to directly image and perturb Rho GTPase signaling without problematic spectral overlap.

Why it works: The abstract states that the red-shifted miRFP720 and the fully NIR miRFP670-miRFP720 FRET pair enabled biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools, allowing simultaneous readout and perturbation.

Rac1 GTPase activity sensingRhoA-Rac1 antagonismRac1-GDI binding coordinationupstream Rac1 activationnear-infrared FRET biosensor designmultiplexed fluorescence imagingoptogenetic perturbation

Taxonomy & Function

Primary hierarchy

Mechanism Branch

Architecture: A reusable architecture pattern for arranging parts into an engineered system.

Techniques

No technique tags yet.

Target processes

signaling

Input: Light

Implementation Constraints

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

Use requires expression of the NIR Rac1 biosensor construct and imaging of near-infrared FRET signals. The reported experiments combined it with CFP-YFP FRET biosensors and the LOV-TRAP optogenetic system, indicating practical compatibility with multiplexed fluorescent and light-control setups.

The supplied evidence does not provide quantitative performance metrics such as dynamic range, kinetics, photostability, or signal-to-noise. It also does not indicate independent replication beyond the originating study, and the biosensor is described as a reporter rather than a direct actuator of Rac1.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 2application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 3application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 4application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 5application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 6application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 7application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 8application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 9application demosupports2018Source 1needs review

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1
Claim 10biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 11biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 12biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 13biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 14biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 15biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 16biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 17biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 18biological observationsupports2018Source 1needs review

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules
Claim 19biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 20biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 21biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 22biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 23biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 24biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 25biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 26biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 27biological observationsupports2018Source 1needs review

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK
Claim 28tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 29tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 30tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 31tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 32tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 33tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 34tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 35tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 36tool capabilitysupports2018Source 1needs review

miRFP720 and the miRFP670-miRFP720 fully near-infrared FRET pair enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.

Here we report the most red-shifted monomeric near-infrared (NIR) fluorescent protein, miRFP720, and the fully NIR Förster resonance energy transfer (FRET) pair miRFP670-miRFP720, which together enabled design of biosensors compatible with CFP-YFP imaging and blue-green optogenetic tools.
Claim 37tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 38tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 39tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 40tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 41tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 42tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 43tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 44tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.
Claim 45tool developmentsupports2018Source 1needs review

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

Approval Evidence

1 source4 linked approval claimsfirst-pass slug nir-rac1-biosensor
We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

Source:

application demosupports

The authors simultaneously observed Rac1 activity during optogenetic manipulation of Rac1.

and simultaneously observed Rac1 activity during optogenetic manipulation of Rac1

Source:

biological observationsupports

Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules.

showed that Rac1 activity and GDI binding closely depend on the spatiotemporal coordination between these two molecules

Source:

biological observationsupports

Using the multiplexed imaging setup, the authors directly observed and quantified antagonism between RhoA and Rac1 that depended on the RhoA-downstream effector ROCK.

We directly observed and quantified antagonism between RhoA and Rac1 dependent on the RhoA-downstream effector ROCK

Source:

tool developmentsupports

The authors developed a near-infrared biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

We developed a NIR biosensor for Rac1 GTPase and demonstrated its use in multiplexed imaging and light control of Rho GTPase signaling pathways.

Source:

Comparisons

Source-stated alternatives

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Source-backed strengths

The reported strength is compatibility with direct multiplex imaging and optogenetic experiments involving Rho GTPases. In the cited study, the construct supported simultaneous observation of Rac1 activity during optogenetic manipulation of Rac1 and contributed to the observation that Rac1 activity and GDI binding depend on spatiotemporal coordination.

Source:

supports multiplexed imaging

Source:

compatible with light control experiments

Source:

used concurrently with CFP-YFP FRET biosensors and LOV-TRAP

Compared with biosensors

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Shared frame: source-stated alternative in extracted literature

Strengths here: supports multiplexed imaging; compatible with light control experiments; used concurrently with CFP-YFP FRET biosensors and LOV-TRAP.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Compared with biosensors for active Rho detection

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Shared frame: source-stated alternative in extracted literature

Strengths here: supports multiplexed imaging; compatible with light control experiments; used concurrently with CFP-YFP FRET biosensors and LOV-TRAP.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Compared with CFP-YFP FRET biosensors

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Shared frame: source-stated alternative in extracted literature

Strengths here: supports multiplexed imaging; compatible with light control experiments; used concurrently with CFP-YFP FRET biosensors and LOV-TRAP.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Compared with fluorescent protein based reporters and biosensors

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Shared frame: source-stated alternative in extracted literature

Strengths here: supports multiplexed imaging; compatible with light control experiments; used concurrently with CFP-YFP FRET biosensors and LOV-TRAP.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Compared with FRET

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Shared frame: source-stated alternative in extracted literature

Strengths here: supports multiplexed imaging; compatible with light control experiments; used concurrently with CFP-YFP FRET biosensors and LOV-TRAP.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Compared with genetically engineered biosensors

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Shared frame: source-stated alternative in extracted literature

Strengths here: supports multiplexed imaging; compatible with light control experiments; used concurrently with CFP-YFP FRET biosensors and LOV-TRAP.

Source:

The study combines this biosensor with CFP-YFP FRET biosensors for RhoA and Rac1-GDI binding, indicating those visible-range biosensors as complementary approaches.

Ranked Citations

  1. 1.
    StructuralSource 1Nature Chemical Biology2018Claim 1Claim 2Claim 3

    Extracted from this source document.