Source 1primary paper2015Scientific Reports
Toolkit/CRY2-CIB1 optogenetic PIP3 production system
CRY2-CIB1 optogenetic PIP3 production system
Also known as: CRY2-CIB1 optogenetic system, optogenetic system
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The CRY2-CIB1 optogenetic PIP3 production system is a blue-light-responsive multi-component switch built from Arabidopsis CRY2 and CIB1. It recruits a CRY2-fused constitutively active PI3-kinase from the cytosol to the plasma membrane through light-induced CRY2-CIB1 interaction, enabling sub-second spatiotemporal control of PIP3 production.
Usefulness & Problems
Why this is useful
This system is useful for perturbing phosphatidylinositol (3,4,5)-trisphosphate signaling with high temporal and spatial precision using light. The cited work indicates that it was designed to visualize PIP3 production on a sub-second timescale and to interrogate temporal dynamics linked to Akt signaling.
Problem solved
It addresses the problem of controlling and observing plasma-membrane PIP3 generation with precise spatiotemporal resolution. The reported localized light stimulation was associated with real-time cell movements, indicating utility for linking local PIP3 production to rapid cellular responses.
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Mechanisms
induced enzymatic activation via subcellular relocalizationlight-driven membrane recruitmentlight-induced heterodimerizationTechniques
Computational DesignTarget processes
signalingInput: Light
Implementation Constraints
The construct architecture described in the evidence uses Arabidopsis CRY2 and CIB1, with CRY2 fused to a constitutively active PI3-kinase that is cytosolic before illumination and recruited to the plasma membrane after blue light exposure. The available evidence does not specify additional construct details, expression systems, membrane anchor design, or cofactor requirements.
The supplied evidence does not provide quantitative performance metrics such as dynamic range, reversibility kinetics, light dose requirements, or background activity in the dark. It also does not specify the exact PI3-kinase construct, host cell types, or breadth of validation across biological contexts.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Source 2primary paper2021Chinese Journal of Chemistry
Ranked Claims
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
timescale sub-second
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
PIP3 production is visualized by translocation of the GRP1 PH domain from the cytosol to the plasma membrane with high specificity.
The PIP3 production is visualized via a fused fluorescent protein by the translocation of a Pleckstrin Homology (PH) domain (GRP1) from the cytosol to the plasma membrane with high specificity.
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
Approval Evidence
2 sources5 linked approval claimsfirst-pass slugs cry2-cib1-optogenetic-pip3-production-system, optogenetic-system
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
Source:
An optogenetic system for interrogating the temporal dynamics of Akt
Source:
cellular responsesupports
Localized light stimulation was associated with real-time cell movements.
Notably, the real-time cell movements were also observed upon localized light stimulation.
Source:
design capabilitysupports
The authors designed an optogenetic CRY2-CIB1 system to spatiotemporally visualize PIP3 production with sub-second timescale.
Herein, we design an optogenetic system that uses light sensitive protein-protein interaction between Arabidopsis cryptochrome 2 (CRY2) and CIB1 to spatiotemporally visualize the PIP3 production with sub-second timescale.
Source:
mechanismsupports
In the system, blue light drives CRY2 fused to constitutively active PI3-kinase from the cytosol to the plasma membrane through CRY2-CIB1 interaction.
In this system, a CIBN is anchored on the plasma membrane, whereas a CRY2 fused with a constitutively active PI3-kinase (acPI3K) would be driven from the cytosol to the membrane by the blue-light-activated CRY2-CIB1 interaction upon light irradiation.
Source:
performancesupports
The optogenetic system initiates PIP3 synthesis on the plasma membrane with fast dynamics and reversibility.
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
Source:
study purposesupports
The paper reports an optogenetic system intended to interrogate the temporal dynamics of Akt.
Source:
Comparisons
Source-backed strengths
A key strength is sub-second spatiotemporal control of PIP3 production enabled by blue-light-triggered recruitment of constitutively active PI3-kinase to the plasma membrane. The literature also reports localized stimulation associated with real-time cell movements, supporting functional coupling between optical input and cellular behavior.
Source:
We demonstrated the fast dynamics and reversibility of the optogenetic system initiated PIP3 synthesis on the plasma membrane.
Ranked Citations
- 1.
- 2.