Source 1primary paper2021Nature Communications
Toolkit/LOV2 module
LOV2 module
Also known as: light-inducible LOV2 module
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The LOV2 module is a light-inducible protein domain incorporated into the FERM domain of an engineered focal adhesion kinase (FAK). In the reported 2021 Nature Communications system, it provides optogenetic input to an allosterically regulated single-protein two-input OR gate while preserving overall FAK domain architecture.
Usefulness & Problems
Why this is useful
This module is useful as a light-responsive regulatory element for controlling signaling proteins within a single engineered polypeptide. In the reported FAK design, it enables optical control as one of two orthogonal inputs combined with chemogenetic regulation.
Problem solved
It helps solve the problem of integrating light-based control into a single-protein signaling actuator without disrupting the overall architecture of FAK. In the cited system, this supports construction of an allosterically regulated two-input OR logic gate in living cells.
Problem links
Need conditional control of signaling activity
DerivedThe LOV2 module is a light-inducible protein domain inserted into the FERM domain of engineered focal adhesion kinase (FAK). In the reported system, it contributes optogenetic control to an allosterically regulated single-protein two-input OR gate while preserving overall FAK domain architecture.
Need precise spatiotemporal control with light input
DerivedThe LOV2 module is a light-inducible protein domain inserted into the FERM domain of engineered focal adhesion kinase (FAK). In the reported system, it contributes optogenetic control to an allosterically regulated single-protein two-input OR gate while preserving overall FAK domain architecture.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
allosteric switchingallosteric switchingoptogenetic regulationoptogenetic regulationorthogonal multi-input regulationorthogonal multi-input regulationTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: regulatorswitch architecture: uncaging
The available evidence indicates that the LOV2 module was inserted in the FERM domain of engineered FAK and paired with a rapamycin-inducible uniRapR module in the kinase domain. No additional construct design details, cofactors, expression systems, or delivery methods are provided in the supplied evidence.
The supplied evidence only documents the LOV2 module in one engineered FAK context and does not provide standalone performance metrics such as activation wavelength, dynamic range, kinetics, or reversibility. Independent replication and broader validation across proteins, cell types, or organisms are not established from the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
Dynamic FAK activation increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
We demonstrate that dynamic FAK activation profoundly increased cell multiaxial complexity in the fibrous extracellular matrix microenvironment and decreased cell motility.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
An engineered single protein design was allosterically regulated to function as a two-input logic OR gate.
we report an engineered, single protein design that is allosterically regulated to function as a 'two-input logic OR gate'
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
The work provides proof-of-principle for fine multimodal control of protein function.
This work provides proof-of-principle for fine multimodal control of protein function
Approval Evidence
1 source2 linked approval claimsfirst-pass slug lov2-module
a light-inducible LOV2 module in the FERM domain
Source:
design architecturesupports
The engineered focal adhesion kinase system uses chemo- and optogenetic regulation with a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain while retaining FAK domain architecture.
Our system is based on chemo- and optogenetic regulation of focal adhesion kinase. In the engineered FAK, all of FAK domain architecture is retained and key intramolecular interactions between the kinase and the FERM domains are externally controlled through a rapamycin-inducible uniRapR module in the kinase domain and a light-inducible LOV2 module in the FERM domain.
Source:
orthogonal regulationsupports
Chemo- and optogenetic switches enabled orthogonal regulation of protein function in the engineered system.
Orthogonal regulation of protein function was possible using the chemo- and optogenetic switches.
Source:
Comparisons
Source-backed strengths
The reported design places the LOV2 module in the FERM domain while retaining FAK domain architecture. Within that engineered system, dynamic FAK activation was associated with increased cell multiaxial complexity in a fibrous extracellular matrix microenvironment and decreased cell motility.
Compared with AsLOV2-Jα
LOV2 module and AsLOV2-Jα address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: allosteric switching; same primary input modality: light
Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.
LOV2 module and photoactivatable inhibitor for cyclic-AMP dependent kinase (PKA) address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: allosteric switching; same primary input modality: light
Compared with uniRapR module
LOV2 module and uniRapR module address a similar problem space because they share signaling.
Shared frame: same top-level item type; shared target processes: signaling; shared mechanisms: allosteric switching, orthogonal multi-input regulation; same primary input modality: light
Ranked Citations
- 1.