Source 1primary paper2023Journal of Biological Chemistry
Toolkit/reversible optogenetic unmasking-masking of Ct residues
reversible optogenetic unmasking-masking of Ct residues
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
Reversible optogenetic unmasking-masking of carboxy-terminal residues is an engineering method used to probe how exposed versus occluded C-terminal sequence features affect prenylation and membrane interactions of prenylated proteins. In the cited work, it was applied to G protein gamma (Gγ) C-terminal residues to enable light-controlled interrogation of their functional contribution.
Usefulness & Problems
Why this is useful
This method is useful for testing whether specific carboxy-terminal residues contribute to prenylation efficiency and membrane association in a reversible, light-controlled manner. The cited study used it to examine how C-terminal sequence context in Gγ proteins influences prenylation-related behavior under suboptimal conditions.
Problem solved
It addresses the problem of experimentally isolating the contribution of C-terminal residues adjacent to prenylation motifs to protein prenylation and membrane interactions. The evidence indicates that a few hydrophobic and charged carboxy-terminal residues can be crucial determinants of prenylation ability under suboptimal conditions, motivating a method that can selectively expose or mask these residues.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete method used to build, optimize, or evolve an engineered system.
Mechanisms
optogenetic masking/unmaskingreversible light-controlled exposure of carboxy-terminal residuesTechniques
No technique tags yet.
Target processes
signalingInput: Light
Implementation Constraints
The available evidence indicates an optogenetic, reversible masking/unmasking design applied to carboxy-terminal residues, consistent with a domain-fusion-based construct strategy. However, the supplied material does not specify the photosensory module, illumination parameters, expression system, or any required cofactors.
The supplied evidence supports application in the context of prenylated proteins, specifically Gγ polypeptides, but does not establish performance across diverse protein classes or cellular systems. No quantitative performance metrics, wavelength details, construct architecture, or independent replication are provided in the supplied evidence.
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Approval Evidence
1 source3 linked approval claimsfirst-pass slug reversible-optogenetic-unmasking-masking-of-ct-residues
Reversible optogenetic unmasking-masking of Ct residues was used to probe their contribution to prenylation and membrane interactions of the prenylated proteins.
Source:
determinant of activitysupports
A few hydrophobic and charged residues at the carboxy terminus are crucial determinants of protein prenylation ability under suboptimal conditions.
Our results also show a few hydrophobic and charged residues at the Ct are crucial determinants of a protein's prenylation ability, especially under suboptimal conditions.
Source:
mechanistic effectsupports
Specific carboxy-terminal residues regulate membrane interactions, statin sensitivity, and extent of prenylation of G protein gamma polypeptides.
Our findings suggest that specific Ct residues regulate membrane interactions of the Gγ polypeptide, statin sensitivity, and extent of prenylation.
Source:
mechanistic implicationsupports
Differences in Gγ subtype composition may allow statins to differentially perturb heterotrimeric G protein signaling across cells.
Given the cell and tissue-specific expression of different Gγ subtypes, our findings indicate a plausible mechanism allowing for statins to differentially perturb heterotrimeric G protein signaling in cells depending on their Gγ-subtype composition.
Source:
Comparisons
Source-backed strengths
The method provides reversible, optogenetic control over exposure of carboxy-terminal residues, allowing direct probing of their role in prenylation and membrane interactions. In the cited context, it was informative for Gγ proteins, whose specific carboxy-terminal residues were linked to membrane interactions, statin sensitivity, and extent of prenylation.
Ranked Citations
- 1.