Toolkit/LOV-based optogenetic devices

LOV-based optogenetic devices

Construct Pattern·Research·Since 2015

Also known as: optogenetic tools

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

Summary

LOV-based optogenetic devices are engineered tools built from small, light-responsive LOV modules to confer photoregulated control of cellular signaling. The supplied evidence supports their role as a general platform for optogenetic tool construction but does not specify individual device architectures or target proteins.

Usefulness & Problems

Why this is useful

These devices are useful because LOV modules provide a compact light-responsive platform for engineering optical control over signaling processes. The cited source frames them as a means to impart photoregulated control, although quantitative performance or application-specific outcomes are not provided in the supplied evidence.

Problem solved

LOV-based optogenetic devices address the need to control cellular signaling with light rather than constitutive or non-optical inputs. The evidence also indicates that engineering this control is challenged by achieving high sensitivity together with fast on/off kinetics across divergent LOV photocycles.

Taxonomy & Function

Primary hierarchy

Mechanism Branch

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

Target processes

signaling

Input: Light

Implementation Constraints

The supplied evidence establishes LOV modules as the core light-responsive component used to build these devices. However, it does not provide practical details on cofactors, expression systems, delivery methods, wavelengths, or construct architectures.

Construction of highly sensitive devices with fast on/off kinetics is complicated by divergent photocycle properties among LOV family members. Design and implementation are also hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1knowledge gapsupports2021Source 2needs review

Further improvements in Rho-control and Rho-detection tools are needed to reveal the role of other Rho GTPases in cytokinesis and to identify molecular mechanisms controlling Rho activity.

Claim 2review summarysupports2021Source 2needs review

Recent optogenetic tools and biosensors that control and detect active Rho have overcome some of these challenges and are helping elucidate the role of RhoA in cytokinesis.

Claim 3engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 4engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 5engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 6engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 7engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 8engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 9engineering constraintsupports2015Source 1needs review

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.
Claim 10engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 11engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 12engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 13engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 14engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 15engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 16engineering limitationsupports2015Source 1needs review

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.
Claim 17platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 18platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 19platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 20platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 21platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 22platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 23platform potentialsupports2015Source 1needs review

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Claim 24review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.
Claim 25review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.
Claim 26review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.
Claim 27review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.
Claim 28review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.
Claim 29review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.
Claim 30review focusneutral2015Source 1needs review

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.

Approval Evidence

2 sources6 linked approval claimsfirst-pass slugs lov-based-optogenetic-devices, optogenetic-tools-for-rho-gtpase-control
The recent generation of optogenetic tools and biosensors that control and detect active Rho has overcome some of these challenges and is helping to elucidate the role of RhoA in cytokinesis.

Source:

LOV-based optogenetic devices: light-driven modules to impart photoregulated control of cellular signaling... The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.

Source:

knowledge gapsupports

Further improvements in Rho-control and Rho-detection tools are needed to reveal the role of other Rho GTPases in cytokinesis and to identify molecular mechanisms controlling Rho activity.

Source:

review summarysupports

Recent optogenetic tools and biosensors that control and detect active Rho have overcome some of these challenges and are helping elucidate the role of RhoA in cytokinesis.

Source:

engineering constraintsupports

Divergent photocycle properties among LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Source:

engineering limitationsupports

Design and implementation of LOV-based optogenetic devices are hindered by incomplete understanding of how light-driven allosteric conformational changes activate diverse signal transduction domains.

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.

Source:

platform potentialsupports

LOV modules are presented as a platform for constructing optogenetic tools.

The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.

Source:

review focusneutral

The review focuses on tuning LOV domain chemistry and signal transduction to improve optogenetic tools.

In the present review we discuss the history of LOV domain research with primary emphasis on tuning LOV domain chemistry and signal transduction to allow for improved optogenetic tools.

Source:

Comparisons

Source-backed strengths

A key strength supported by the evidence is that LOV modules are small and light responsive, making them a versatile platform for optogenetic engineering. The source specifically positions them for photoregulated control of cellular signaling, but no comparative benchmarks or validation data are included here.

Source:

Further, divergent photocycle properties amongst LOV family members complicate construction of highly sensitive devices with fast on/off kinetics.

Source:

Currently, the design and implementation of these devices is partially hindered by a lack of understanding of how light drives allosteric changes in protein conformation to activate diverse signal transduction domains.

Ranked Citations

  1. 1.
    StructuralSource 1Frontiers in Molecular Biosciences2015Claim 3Claim 4Claim 5

    Seeded from load plan for claim cl1. Extracted from this source document.

  2. 2.
    StructuralSource 2Small GTPases2021Claim 1Claim 2

    Seeded from load plan for claim cl2. Extracted from this source document.