Source 1primary paper2021Nature Communications
Toolkit/OptoMYPT
OptoMYPT
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
OptoMYPT is a blue-light-controlled multi-component optogenetic switch that couples the PP1c-binding domain of MYPT1 to an optogenetic dimerizer to recruit endogenous protein phosphatase 1c to the plasma membrane. This recruitment induces dephosphorylation of myosin regulatory light chains and reduces actomyosin contractile force.
Usefulness & Problems
Why this is useful
OptoMYPT enables acute optical relaxation of actomyosin contractility by controlling endogenous PP1c localization with light. In the cited study, this allowed perturbation of cortical tension during cytokinesis and revealed that relaxing cortical tension at both poles accelerates furrow ingression.
Source:
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Source:
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
Source:
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
Problem solved
This tool addresses the need for spatiotemporal manipulation of myosin II-dependent contractility without directly engineering the endogenous phosphatase catalytic subunit. It specifically provides a way to decrease cortical tension through light-dependent membrane recruitment of endogenous PP1c and consequent myosin regulatory light chain dephosphorylation.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
dephosphorylationHeterodimerizationlight-dependent membrane recruitmentphosphatase recruitmentPhotocleavageTechniques
No technique tags yet.
Target processes
localizationrecombinationInput: Light
Implementation Constraints
OptoMYPT is implemented by fusing the PP1c-binding domain of MYPT1 to an optogenetic dimerizer to achieve light-dependent recruitment of endogenous PP1c to the plasma membrane. The available evidence supports blue-light activation and membrane recruitment, but does not specify the dimerizer system, host cells, or cofactor requirements.
The supplied evidence is limited to a single 2021 study and focuses on cytokinesis-related cortical tension, so validation breadth is narrow. The exact optogenetic dimerizer, construct architecture, illumination parameters, and performance metrics are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
Approval Evidence
1 source10 linked approval claimsfirst-pass slug optomypt
The system, named OptoMYPT, combines a catalytic subunit of the type I phosphatase-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
Source:
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
Source:
activity effectsupports
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases actomyosin contractile force.
Blue-light illumination is sufficient to induce dephosphorylation of myosin regulatory light chains and a decrease in actomyosin contractile force in mammalian cells and Xenopus embryos.
Source:
biological insightsupports
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Source:
biological insightsupports
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We find that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Source:
biological mechanismsupports
Cortical tension substantially antagonizes constriction of the cleavage furrow during cytokinesis.
revealing that the cortical tension substantially antagonizes constriction of the cleavage furrow
Source:
biological mechanismsupports
Relaxation of cortical tension at both poles by OptoMYPT accelerates furrow ingression rate during cytokinesis.
We found that the relaxation of cortical tension at both poles by OptoMYPT accelerated the furrow ingression rate
Source:
functional effectsupports
Blue-light illumination with OptoMYPT induces dephosphorylation of myosin regulatory light chains and decreases traction force at the subcellular level.
Blue-light illumination was sufficient to induce dephosphorylation of myosin regulatory light chains and decrease in traction force at the subcellular level.
Source:
mechanismsupports
OptoMYPT combines a PP1c-binding domain of MYPT1 with an optogenetic dimerizer to enable light-dependent recruitment of endogenous PP1c to the plasma membrane.
The system, named OptoMYPT, combines a protein phosphatase 1c (PP1c)-binding domain of MYPT1 with an optogenetic dimerizer, so that it allows light-dependent recruitment of endogenous PP1c to the plasma membrane.
Source:
mechanismsupports
OptoMYPT enables light-dependent recruitment of endogenous PP1c to the plasma membrane.
it allows light-dependent recruitment of endogenous PP1c to the plasma membrane
Source:
tool functionsupports
OptoMYPT is an optogenetic method that induces relaxation of actomyosin contractility at the subcellular level.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility at the subcellular level. The system, named OptoMYPT
Source:
tool introductionsupports
OptoMYPT is an optogenetic method for inducing relaxation of actomyosin contractility.
Here, we demonstrate an optogenetic method to induce relaxation of actomyosin contractility. The system, named OptoMYPT
Source:
Comparisons
Source-backed strengths
The reported system acts through endogenous PP1c recruitment, linking optical input to a defined biochemical output: myosin regulatory light chain dephosphorylation. It was functionally validated by decreased actomyosin contractile force and by a cytokinesis phenotype in which pole relaxation accelerated furrow ingression.
Ranked Citations
- 1.