Source 1primary paper2014ACS Synthetic Biology
Toolkit/photoactivatable inhibitor for cyclic-AMP dependent kinase (PKA)
photoactivatable inhibitor for cyclic-AMP dependent kinase (PKA)
Also known as: PKA photoactivatable inhibitor
Taxonomy: Mechanism Branch / Component. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The photoactivatable inhibitor for cyclic-AMP dependent kinase (PKA) is a LOV2-based photoswitchable inhibitory peptide engineered to control endogenous PKA activity with light in living cells. It functions by coupling a kinase-inhibitory peptide to the LOV2 Jα helix so that inhibition is light dependent.
Usefulness & Problems
Why this is useful
This tool enables optical control of endogenous PKA signaling in living cells rather than relying on constitutively active inhibitors. The source study reports that these photoswitchable inhibitors 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 achieving reversible, light-dependent inhibition of endogenous kinase activity, specifically PKA, inside living cells. The reported design converts a kinase inhibitor into a photoswitchable form whose activity depends on illumination state.
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 an inhibitory peptide to the LOV2 Jα helix, indicating a domain-fusion architecture based on a LOV2 photosensory module. The evidence supports use in living cells, but the supplied material does not specify construct sequence, expression system, chromophore requirements, or illumination parameters.
The provided evidence is limited to a single source and does not report quantitative performance metrics such as dynamic range, kinetics, wavelength dependence, or reversibility for the PKA-specific construct. Independent replication and validation across organisms, cell types, or in vivo settings are not documented in the supplied 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-cyclic-amp-dependent-kinase-pka
Photoactivatable inhibitors for cyclic-AMP dependent kinase (PKA)
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 source literature describes LOV2-based analogues of kinase inhibitors with light-dependent activity. Inhibitory peptides appended to the Jα helix potently inhibited kinases in the light, and the constructs 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.