Source 1primary paper2013Cytoskeleton
Toolkit/Diaphanous Autoregulatory Domain from mDia1
Diaphanous Autoregulatory Domain from mDia1
Also known as: isolated Diaphanous Autoregulatory Domain from mDia1
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The Diaphanous Autoregulatory Domain from mDia1, in this tool context, is an optogenetic fusion between the Avena sativa Phototropin1 LOV2 domain and an isolated mDia1 DAD. Blue light uncages the DAD, enabling rapid activation of endogenous diaphanous-related formins and acute actin cytoskeletal remodeling.
Usefulness & Problems
Why this is useful
This tool is useful for temporally precise optical control of endogenous diaphanous-related formin activity rather than overexpressing full-length actin regulators. In the reported study, photoactivation induced filopodia and lamellipodia formation and increased F-actin along existing stress fibers within minutes.
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
It addresses the problem of acutely activating endogenous diaphanous-related formins with light while keeping the construct inactive in the dark. The reported application also enabled interrogation of how formin-driven F-actin accumulation relates to stress-fiber contractility.
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.
Problem links
Need precise spatiotemporal control with light input
DerivedThis tool is an optogenetic fusion of the Avena sativa Phototropin1 LOV2 domain to an isolated Diaphanous Autoregulatory Domain (DAD) from mDia1. Blue-light activation uncages the DAD and rapidly activates endogenous diaphanous-related formins, producing acute actin cytoskeletal remodeling.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
activation of endogenous diaphanous-related forminsactivation of endogenous diaphanous-related forminsallosteric switchingallosteric switchinglight-dependent uncaginglight-dependent uncagingTechniques
No technique tags yet.
Target processes
No target processes tagged yet.
Input: Light
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: spectral hardware requirementoperating role: actuatoroperating role: reporterswitch architecture: uncaging
The construct is based on domain fusion of the Avena sativa Phototropin1 LOV2 domain to an isolated mDia1 Diaphanous Autoregulatory Domain. Its input modality is blue light, and the reported design relies on light-dependent uncaging of the DAD to activate endogenous diaphanous-related formins. No additional implementation details such as expression system, linker design, or cofactor requirements are provided in the supplied evidence.
The available evidence is from a single 2013 study and focuses on cytoskeletal phenotypes, with limited information here on quantitative dynamic range, reversibility, or cell-type breadth. The mechanistic conclusion about decoupling between F-actin accumulation and contractility is presented as an interpretation rather than a universally established property.
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
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 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
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.
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
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 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 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
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 diaphanous-autoregulatory-domain-from-mdia1
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
The reported construct was inactive in the dark and rapidly activated endogenous diaphanous-related formins under blue light. In cells, activation produced fast, observable actin remodeling, including filopodia, lamellipodia, and increased F-actin along stress fibers within minutes. The study further reported stress-fiber thickening without an increase in contractility.
Compared with CRY2 C-terminal tail
Diaphanous Autoregulatory Domain from mDia1 and CRY2 C-terminal tail address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: allosteric switching; same primary input modality: light
Diaphanous Autoregulatory Domain from mDia1 and photoactivatable inhibitor for cyclic-AMP dependent kinase (PKA) address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: allosteric switching; same primary input modality: light
Compared with Vivid (VVD) LOV domain
Diaphanous Autoregulatory Domain from mDia1 and Vivid (VVD) LOV domain address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: allosteric switching; same primary input modality: light
Ranked Citations
- 1.