Source 1review2015Frontiers in Molecular Biosciences
Toolkit/Light-Oxygen-Voltage domain
Light-Oxygen-Voltage domain
Also known as: LOV domain, LOV domains, LOV modules
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Light-Oxygen-Voltage (LOV) domains are small, light-responsive protein modules found in algae, plants, bacteria, and fungi that function as blue-light sensors controlling cellular responses to light. They are presented as a platform for constructing optogenetic tools that confer photoregulated control of cellular signaling.
Usefulness & Problems
Why this is useful
LOV domains are useful as compact sensory modules for building optogenetic systems that respond to blue light. Their value lies in providing a biologically widespread, light-responsive domain family that can be incorporated into tools for photoregulated control of signaling.
Source:
Algae, plants, bacteria and fungi contain Light-Oxygen-Voltage (LOV) domains that function as blue light sensors to control cellular responses to light.
Problem solved
LOV domains help address the need for genetically encoded modules that couple light input to control of cellular signaling. The cited work specifically frames them as a platform for constructing optogenetic devices, although detailed application-specific performance is not provided in the supplied evidence.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
allosteric conformational changeblue-light sensingconformational uncagingConformational UncagingTechniques
Computational DesignTarget processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The supplied evidence supports blue light as the input modality and identifies LOV domains as protein modules used in optogenetic device construction. However, the evidence does not specify cofactors, expression systems, delivery methods, or particular construct architectures.
Construction of highly sensitive LOV-based 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
Source 2primary paper2014PLoS ONE
Ranked Claims
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
LOV domains function as blue light sensors that control cellular responses to light.
Algae, plants, bacteria and fungi contain Light-Oxygen-Voltage (LOV) domains that function as blue light sensors to control cellular responses to light.
LOV domains contain a bound flavin chromophore that is reduced upon photon absorption and forms a reversible metastable covalent bond with a nearby cysteine residue.
All LOV domains contain a bound flavin chromophore that is reduced upon photon absorption and forms a reversible, metastable covalent bond with a nearby cysteine residue.
Approval Evidence
2 sources6 linked approval claimsfirst-pass slug light-oxygen-voltage-domain
The Light-Oxygen-Voltage domain family of proteins is widespread in biology... The small, light responsive LOV modules offer a novel platform for the construction of optogenetic tools.
Source:
Algae, plants, bacteria and fungi contain Light-Oxygen-Voltage (LOV) domains that function as blue light sensors to control cellular responses to light.
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:
functionsupports
LOV domains function as blue light sensors that control cellular responses to light.
Algae, plants, bacteria and fungi contain Light-Oxygen-Voltage (LOV) domains that function as blue light sensors to control cellular responses to light.
Source:
mechanismsupports
LOV domains contain a bound flavin chromophore that is reduced upon photon absorption and forms a reversible metastable covalent bond with a nearby cysteine residue.
All LOV domains contain a bound flavin chromophore that is reduced upon photon absorption and forms a reversible, metastable covalent bond with a nearby cysteine residue.
Source:
Comparisons
Source-backed strengths
The evidence describes LOV modules as small and light responsive, properties that support their use as engineering components in optogenetic tool construction. They are also widespread across algae, plants, bacteria, and fungi, indicating a broadly occurring class of blue-light sensory domains.
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.