Source 1primary paper2022Journal of Biological Chemistry
Toolkit/blue light-activated PKC isozyme recruitment system
blue light-activated PKC isozyme recruitment system
Also known as: CRY2-CIB1-based PKC recruitment system, optogenetic blue light-activated PKC isozyme
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The blue light-activated PKC isozyme recruitment system is a multi-component optogenetic switch that uses the plant-derived CRY2-CIB1 interaction to recruit PKC isozyme catalytic domains to the cell surface under blue light. In the reported format, CRY2-tagged PKC catalytic domains undergo light-triggered membrane translocation, and a PKCε implementation robustly activates GIRK1/4 potassium channels.
Usefulness & Problems
Why this is useful
This system provides a direct optical method to position individual PKC isozyme catalytic domains at the plasma membrane, enabling targeted phosphorylation of membrane proteins. The reported GIRK1/4 activation result indicates utility for dissecting isozyme-specific PKC signaling with temporal control by blue light.
Source:
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Source:
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
Problem solved
It addresses the problem of delivering a reliable and direct stimulus for membrane-localized PKC phosphorylation events without relying on broader endogenous activation pathways. The source also states that the approach is anticipated to be extendable to other PKC isoforms for targeted membrane protein phosphorylation.
Source:
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Source:
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
Heterodimerizationinduced subcellular translocationlight-induced heterodimerizationproximity-driven membrane protein phosphorylationTechniques
No technique tags yet.
Target processes
localizationtranscriptionInput: Light
Implementation Constraints
The construct design described in the evidence tags CRY2 to the catalytic domain of PKC isozymes and uses the N terminus of CIB1 as the blue light-responsive binding partner. Blue light is the input modality, and the operational output is induced translocation of the PKC catalytic module to the cell surface; the supplied evidence does not specify expression system, membrane anchor architecture, or cofactor requirements.
The supplied evidence documents functional validation specifically for PKCε and states only an anticipated generalizability to other PKC isoforms, so broader isozyme performance remains unproven here. The evidence set does not provide quantitative kinetics, reversibility, dynamic range, or validation across multiple cell types or targets.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
Approval Evidence
1 source4 linked approval claimsfirst-pass slug blue-light-activated-pkc-isozyme-recruitment-system
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1).
Source:
anticipated generalizabilityneutral
The authors anticipate that the approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation.
We anticipate that this approach can be utilized for other PKC isoforms to provide a reliable and direct stimulus for targeted membrane protein phosphorylation by the relevant PKCs.
Source:
application resultsupports
Using PKCε in this optogenetic system leads to robust activation of GIRK1/4 potassium channels.
We demonstrate this system using PKCε and show that this leads to robust activation of a K+ channel (G protein-gated inwardly rectifying K+ channels 1 and 4)
Source:
mechanism of actionsupports
Tagging CRY2 with the catalytic domain of PKC isozymes efficiently promotes translocation to the cell surface upon blue light exposure.
We show that tagging CRY2 with the catalytic domain of PKC isozymes can efficiently promote its translocation to the cell surface upon blue light exposure.
Source:
tool developmentsupports
The authors developed an optogenetic blue light-activated PKC isozyme system based on CRY2-CIB1 dimerization.
Here, we developed an optogenetic blue light-activated PKC isozyme that harnesses a plant-based dimerization system between the photosensitive cryptochrome-2 (CRY2) and the N terminus of the transcription factor calcium and integrin-binding protein 1 (CIB1)
Source:
Comparisons
Source-backed strengths
The mechanism is explicitly based on blue light-induced CRY2-CIB1 dimerization, which efficiently promotes translocation of CRY2-tagged PKC catalytic domains to the cell surface. Functional validation was reported for PKCε, where deployment in this system led to robust activation of GIRK1/4 potassium channels.
Ranked Citations
- 1.