Source 1primary paper2014ACS Synthetic Biology
Toolkit/membrane-tethered CRY2
membrane-tethered CRY2
Taxonomy: Mechanism Branch / Architecture. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Membrane-tethered CRY2 is a CRY2/CIB optical dimerization configuration in which CRY2 is localized at a membrane to control recruitment of CIB-linked partners with light. The reported application demonstrates that this arrangement is functional and may provide improved local control of protein interactions.
Usefulness & Problems
Why this is useful
This configuration is useful for spatially restricted optogenetic control because it places the CRY2 photoswitch at a membrane rather than in a diffuse cellular compartment. The cited study specifically suggests that membrane tethering may improve local control of protein interactions.
Source:
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
Problem solved
It addresses the problem of controlling where light-induced CRY2/CIB interactions occur inside the cell. The reported use case indicates that membrane localization can be used to constrain inducible dimerization to a defined subcellular site.
Source:
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
Taxonomy & Function
Primary hierarchy
Mechanism Branch
Architecture: A composed arrangement of multiple parts that instantiates one or more mechanisms.
Techniques
No technique tags yet.
Target processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationimplementation constraint: multi component delivery burdenoperating role: actuatorswitch architecture: multi componentswitch architecture: recruitment
Implementation requires a multi-component CRY2/CIB design in which CRY2 is fused to a membrane-targeting element and the interaction partner is linked to CIB. The supplied evidence does not specify the membrane anchor, host system for this configuration, or detailed construct design.
Evidence for this specific membrane-tethered configuration is limited to a brief application statement from a single benchmarking study. Quantitative performance metrics, membrane identity, construct architecture, illumination parameters, and validation across organisms or assays are not provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 showed slightly less background activity in the dark than the TULIP system during regulation of a yeast MAPK signaling pathway.
with slightly less background activity in the dark observed with CRY2/CIB
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
CRY2/CIB1 and TULIPs showed similar responses in a yeast transcriptional assay.
but similar responses between the CRY2/CIB and TULIP systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
The red-light-regulated systems phyB/PIF3 and phyB/PIF6 showed significant differences in light sensitivity and fold-activation levels in a yeast transcriptional assay.
Using a yeast transcriptional assay, we find significant differences in light sensitivity and fold-activation levels between the red light regulated systems
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
CRY2/CIB1 and TULIP systems showed similar responses when used to regulate a yeast MAPK signaling pathway.
Further comparison of the ability of the CRY2/CIB1 and TULIP systems to regulate a yeast MAPK signaling pathway also showed similar responses
Approval Evidence
1 source1 linked approval claimfirst-pass slug membrane-tethered-cry2
In addition, we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2
Source:
application demosupports
CRY2/CIB dimerizers were successfully applied using a membrane-tethered CRY2 configuration, which may allow better local control of protein interactions.
we demonstrate successful application of the CRY2/CIB dimerizers using a membrane-tethered CRY2, which may allow for better local control of protein interactions
Source:
Comparisons
Source-backed strengths
The available evidence shows successful application of CRY2/CIB dimerizers in a membrane-tethered CRY2 format. More generally for CRY2/CIB1, the benchmark study reported slightly less dark background than the TULIP system in regulation of a yeast MAPK signaling pathway and similar responses to TULIPs in a yeast transcriptional assay.
Compared with optoPAK1
membrane-tethered CRY2 and optoPAK1 address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Compared with Opto-RhoGEFs
membrane-tethered CRY2 and Opto-RhoGEFs address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
membrane-tethered CRY2 and two-photon-sensitive caging group for gibberellic acid activation address a similar problem space.
Shared frame: same top-level item type; shared mechanisms: heterodimerization
Strengths here: looks easier to implement in practice.
Ranked Citations
- 1.