From Plankton to Primates: How VSP Sequence Diversity Shapes Voltage Sensing
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View abstract on PubMed
Summary
This summary is machine-generated.Voltage-sensing phosphatases (VSPs) are deeply conserved across species for voltage sensing. However, natural sequence variations significantly alter their function and response to membrane voltage changes, impacting genetically encoded voltage indicator (GEVI) design.
Area Of Science
- Biophysics
- Molecular Biology
- Neuroscience
Background
- Voltage-sensing phosphatases (VSPs) are crucial for understanding voltage sensing mechanisms.
- Genetically encoded voltage indicators (GEVIs) are engineered from VSPs for optical voltage detection.
- Natural sequence diversity in VSPs offers insights into functional evolution.
Purpose Of The Study
- To compare VSP voltage-sensing domains (VSDs) from different species to understand how sequence diversity affects function.
- To evaluate the impact of lineage-specific substitutions on VSP voltage-sensing properties.
- To guide the design of improved GEVIs by analyzing VSP behavior.
Main Methods
- Engineered VSP constructs by replacing the phosphatase domain with a fluorescent protein.
- Expressed constructs in cells to enable optical detection of VSD responses.
- Compared voltage-dependent optical signals across VSP orthologs from various species.
Main Results
- All plasma membrane-localized constructs showed voltage-dependent optical signals, confirming conserved voltage sensing.
- Plankton and sea hare VSPs exhibited left-shifted activation ranges.
- Human VSP2 showed poor recovery, improved by a specific arginine substitution.
- Chinese hamster VSP with atypical S4 charges displayed altered fluorescence responses.
Conclusions
- Voltage-dependent signaling is conserved across VSPs, but lineage-specific variations create distinct functional phenotypes.
- Single amino acid changes can significantly alter VSD movement and reporter output.
- VSPs serve as valuable models for studying voltage sensing and optimizing GEVI development.
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