Source 1primary paper2023International Journal of Molecular Sciences
Toolkit/MLCP-BcLOV4
MLCP-BcLOV4
Also known as: myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
MLCP-BcLOV4 is an optogenetic fusion of myosin light chain phosphatase with the Botrytis cinerea light-oxygen-voltage flavoprotein BcLOV4. It was developed to control actomyosin contractility in the Ciona larval epidermis through light-dependent membrane localization and suppression of phosphorylated myosin activity.
Usefulness & Problems
Why this is useful
This tool enables optical control of mechanical force regulation and membrane behavior in cells and developing tissues. In the reported study, it supported subcellular regulation of membrane elongation in Ciona larval epidermal cells and perturbation of contractility-dependent morphogenesis.
Source:
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
Problem solved
MLCP-BcLOV4 addresses the problem of manipulating actomyosin contractility with spatial and temporal precision in vivo. It was specifically developed to suppress actomyosin activity in the Ciona epidermis and to test the role of apical contractility during atrial siphon invagination.
Source:
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
light-dependent membrane localizationmyosin light chain dephosphorylationoptical suppression of actomyosin contractilityTechniques
Computational DesignTarget processes
localizationInput: Light
Implementation Constraints
The construct is a domain fusion between myosin light chain phosphatase and the Botrytis cinerea LOV flavoprotein BcLOV4. Reported use involved optical activation to drive membrane localization, with optimization of activating light intensity in HeLa cells before application in Ciona larval epidermal cells.
The available evidence comes from a single 2023 study and focuses on HeLa cells and Ciona larval epidermis. The supplied evidence does not report broader organismal validation, quantitative kinetic parameters, reversibility metrics, or performance under alternative illumination regimes.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
Approval Evidence
1 source4 linked approval claimsfirst-pass slug mlcp-bclov4
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
Source:
light dependent localization and force regulationsupports
MLCP-BcLOV4 showed light-dependent membrane localization and regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity.
We first validated the light-dependent membrane localization and regulatory efficiency on mechanical forces of the MLCP-BcLOV4 system as well as the optimum light intensity that activated the system in HeLa cells.
Source:
morphogenesis perturbationsupports
Application of MLCP-BcLOV4 during atrial siphon invagination in Ciona larvae suppressed phosphorylated myosin activity on the apical surface, disrupted apical contractility, and caused failure of invagination.
Our results showed that the activity of phosphorylated myosin on the apical surface of atrial siphon primordium cells was suppressed and apical contractility was disrupted, resulting in the failure of the invagination process.
Source:
subcellular regulationsupports
The optimized MLCP-BcLOV4 system was applied in Ciona larval epidermal cells to regulate membrane elongation at the subcellular level.
Then, we applied the optimized MLCP-BcLOV4 system in Ciona larval epidermal cells to realize the regulation of membrane elongation at the subcellular level.
Source:
tool developmentsupports
The study designed and developed MLCP-BcLOV4 as an optogenetic tool to control actomyosin contractility in the Ciona larval epidermis.
we designed and developed a myosin light chain phosphatase fused with a light-oxygen-voltage flavoprotein from Botrytis cinerea (MLCP-BcLOV4) as an optogenetics tool to control actomyosin contractility activity in the Ciona larva epidermis
Source:
Comparisons
Source-backed strengths
The fusion showed light-dependent membrane localization and measurable regulatory efficiency on mechanical forces in HeLa cells, and the authors identified an optimum activating light intensity. In Ciona larvae, its application suppressed phosphorylated myosin activity at the apical surface, disrupted apical contractility, caused failure of invagination, and enabled subcellular regulation of membrane elongation.
Ranked Citations
- 1.