Source 1primary paper2014ACS Synthetic Biology
Toolkit/photoswitchable inhibitory peptides
photoswitchable inhibitory peptides
Also known as: light-dependent kinase inhibitor analogues, photoactivatable inhibitors
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Photoswitchable inhibitory peptides are LOV2-based, light-dependent analogues of kinase inhibitory peptides engineered to control kinase inhibition with illumination. In the reported implementation, inhibitory peptides appended to the LOV2 Jα helix were used to modulate endogenous signaling in living cells, including systems targeting protein kinase A and myosin light chain kinase.
Usefulness & Problems
Why this is useful
This tool enables optical control of endogenous kinase activity in living cells using genetically encoded inhibitory peptide constructs. It is useful for perturbing signaling with light and for linking kinase inhibition to acute cellular outputs such as changes in cell morphodynamics.
Source:
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA) and myosin light chain kinase (MLCK) are described
Problem solved
These constructs address the problem of making peptide-based kinase inhibitors conditionally active rather than constitutively inhibitory. The reported design provides a way to switch inhibition with light while reducing kinase interaction in the dark state through steric blocking.
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
signalingInput: Light
Implementation Constraints
The reported design appends inhibitory peptides to the LOV2 Jα helix to create a photoswitchable inhibitory module. The evidence supports implementations for protein kinase A and myosin light chain kinase in living cells, but the supplied material does not specify construct architecture beyond the Jα fusion, expression system details, or illumination parameters.
The supplied evidence is limited to a single 2014 study and does not provide quantitative performance metrics such as dynamic range, kinetics, reversibility, or wavelength dependence. Validation is described for living-cell signaling perturbation, but broader benchmarking across targets, organisms, or independent studies is not provided here.
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 source3 linked approval claimsfirst-pass slug photoswitchable-inhibitory-peptides
we developed analogues of kinase inhibitors whose activity is light dependent
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:
engineering resultsupports
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.
Source:
mechanismsupports
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.
Source:
Comparisons
Source-backed strengths
The source study reported that these LOV2-based inhibitor analogues were light dependent and altered endogenous signaling in living cells. The constructs also produced light-dependent changes in cell morphodynamics, supporting functional activity in a cellular context.
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.