Source 1primary paper2014ACS Synthetic Biology
Toolkit/photoactivatable inhibitor for myosin light chain kinase (MLCK)
photoactivatable inhibitor for myosin light chain kinase (MLCK)
Also known as: MLCK photoactivatable inhibitor
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The photoactivatable inhibitor for myosin light chain kinase (MLCK) is a LOV2-based inhibitory peptide construct engineered to make MLCK inhibition light dependent. It is designed to manipulate endogenous MLCK activity in living cells through a photoswitchable inhibitory peptide architecture.
Usefulness & Problems
Why this is useful
This tool is useful for optical control of endogenous kinase signaling with temporal precision in living cells. Source evidence indicates that photoswitchable kinase inhibitors, including the MLCK-targeted construct, altered endogenous signaling and produced light-dependent changes in cell morphodynamics.
Source:
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Problem solved
It addresses the problem of making inhibition of endogenous MLCK conditional on light rather than constitutive. The reported design converts a kinase-inhibitory peptide into a light-responsive regulator, enabling perturbation of signaling in living cells.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Component: A low-level protein part used inside a larger architecture that realizes a mechanism.
Mechanisms
light-dependent steric uncaginglov2 conformational photoswitchingpeptide-mediated kinase inhibitionTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
The design uses an inhibitory peptide appended to the LOV2 Jα helix so that kinase interaction is sterically blocked in the dark and enabled in the light. The available evidence supports use in living cells, but it does not specify construct sequence, illumination wavelength, expression system, or delivery method for the MLCK-specific inhibitor.
The supplied evidence identifies MLCK as a target but does not provide MLCK-specific quantitative performance metrics such as dynamic range, kinetics, reversibility, or inhibition constants. Independent replication and validation outside the cited study are not documented in the provided evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
The authors developed LOV2-based analogues of kinase inhibitors whose activity is light dependent.
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light and were sterically blocked from kinase interaction in the dark.
Inhibitory peptides were appended to the Jα helix, where they potently inhibited kinases in the light but were sterically blocked from kinase interaction in the dark.
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Approval Evidence
1 source2 linked approval claimsfirst-pass slug photoactivatable-inhibitor-for-myosin-light-chain-kinase-mlck
Photoactivatable inhibitors for ... myosin light chain kinase (MLCK)
Source:
cellular effectsupports
These photoswitchable inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
These inhibitors altered endogenous signaling in living cells and produced light-dependent changes in cell morphodynamics.
Source:
tool descriptionsupports
Photoactivatable inhibitors for PKA and MLCK are described.
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Source:
Comparisons
Source-backed strengths
The construct belongs to a class of LOV2-based kinase inhibitor analogues whose activity is light dependent. Reported photoswitchable inhibitors potently inhibited kinases in the light, were sterically blocked from kinase interaction in the dark, and were sufficient to alter endogenous signaling and cell morphodynamics in living cells.
Source:
Using the photoresponse of the LOV2 domain of Avena sativa phototropin 1, we developed analogues of kinase inhibitors whose activity is light dependent.
Ranked Citations
- 1.