Source 1primary paper2013Cytoskeleton
Toolkit/light-oxygen-voltage 2 domain of Avena sativa Phototrophin1
light-oxygen-voltage 2 domain of Avena sativa Phototrophin1
Also known as: LOV2 domain of Avena sativa Phototrophin1
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The light-oxygen-voltage 2 (LOV2) domain of Avena sativa Phototrophin1 was used as a blue-light-responsive caging module by fusion to an isolated Diaphanous Autoregulatory Domain (DAD) from mDia1. In this configuration, the LOV2-based construct was inactive in the dark and rapidly activated endogenous diaphanous-related formins upon blue-light illumination, producing acute actin cytoskeletal remodeling.
Usefulness & Problems
Why this is useful
This LOV2 domain is useful as an optogenetic module for temporally controlling endogenous diaphanous-related formin activity with blue light. In the reported fusion, it enabled rapid induction of filopodia, lamellipodia, and increased F-actin along existing stress fibers within minutes, allowing acute perturbation of actin organization.
Source:
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
Source:
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
Problem solved
The tool addresses the problem of achieving reversible, light-gated control over endogenous formin signaling rather than relying on constitutive or non-optical perturbations. The reported application specifically enabled testing how acute formin activation affects F-actin accumulation and stress fiber behavior.
Source:
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
The reported implementation was a fusion of the Avena sativa Phototrophin1 LOV2 domain to an isolated Diaphanous Autoregulatory Domain from mDia1. The construct functioned as a blue-light-responsive caged DAD that was inactive in the dark and activated endogenous diaphanous-related formins upon illumination. No additional construct architecture, cofactor requirements, or delivery details are provided in the supplied evidence.
The supplied evidence describes this LOV2 domain only in the context of a specific fusion to the mDia1 DAD, so performance as a standalone module or in other fusion architectures is not established here. No quantitative information is provided on activation wavelength range beyond blue light, dynamic range, reversibility kinetics, expression constraints, or validation across multiple cell types or organisms.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
Photo-activation of the tool induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
Using an F-actin reporter, we observed filopodia and lamellipodia formation as well as a steady increase in F-actin along existing stress fibers, starting within minutes of photo-activation.
response onset time within minutes
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The caged diaphanous autoregulatory domain was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light.
This "caged" diaphanous auto-regulatory domain was inactive in the dark but in the presence of blue light rapidly activated endogenous diaphanous-related formins.
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
The results suggest a decoupling between F-actin accumulation and contractility in stress fibers.
Our results suggest a decoupling between F-actin accumulation and contractility in stress fibers
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
Photo-activation did not induce formation of new stress fibers.
Interestingly, we did not observe the formation of new stress fibers.
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
A 1.9-fold increase in F-actin along stress fibers was not accompanied by increased myosin II or an apparent increase in tension judged by focal adhesion size.
Remarkably, a 1.9-fold increase in F-actin was not paralleled by an increase in myosin II along stress fibers and the amount of tension generated by the fibers, as judged by focal adhesion size, appeared unchanged.
F-actin increase 1.9 fold
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
The photoactivatable diaphanous autoregulatory domain is useful for studying diaphanous-related formin function in cells.
demonstrate the utility of photoactivatable diaphanous autoregulatory domain for the study of diaphanous-related formin function in cells
Approval Evidence
1 source1 linked approval claimfirst-pass slug light-oxygen-voltage-2-domain-of-avena-sativa-phototrophin1
Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
Source:
tool developmentsupports
The authors developed an optogenetic technique for activation of endogenous diaphanous-related formins based on a LOV2-mDia1 diaphanous autoregulatory domain fusion.
We have developed an optogenetic technique for the activation of diaphanous-related formins. Our approach is based on fusion of the light-oxygen-voltage 2 domain of Avena sativa Phototrophin1 to an isolated Diaphanous Autoregulatory Domain from mDia1.
Source:
Comparisons
Source-backed strengths
Evidence indicates that the LOV2-DAD construct was inactive in the dark and rapidly activated endogenous diaphanous-related formins in blue light. Photoactivation induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes. The associated study further reported thickening of stress fibers without an increase in contractility, supporting its utility for dissecting actin assembly from contractile output.
Ranked Citations
- 1.