Related Experiment Video
Updated: May 18, 2026
09:57
Imaging Membrane Potential with Two Types of Genetically Encoded Fluorescent Voltage Sensors
Published on: February 4, 2016
Voltage-Controlled Enzymes: The New JanusBifrons
1Department of Physiology and Biophysics, Virginia Commonwealth University School of Medicine Richmond, VA, USA.
Frontiers in Pharmacology
|September 21, 2012
Summary
The Ciona intestinalis voltage-sensitive phosphatase (Ci-VSP) links membrane potential to enzymatic activity. This review focuses on Ci-VSP
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- The Ciona intestinalis voltage-sensitive phosphatase (Ci-VSP) is the first identified Voltage-controlled Enzyme (VEnz).
- It uniquely conjugates voltage sensitivity with enzymatic activity in a single protein.
- VSPs offer a model for understanding membrane potential sensing and enzymatic control.
Purpose of the Study:
- To review the electrical activity of Voltage-sensitive phosphatases (VSPs).
- To highlight VSPs as electrically active proteins, distinct from their enzymatic function.
- To explore VSPs as isolated models for studying voltage-sensing domains (VSDs).
Main Methods:
- Review of existing literature on VSPs and their electrical properties.
- Analysis of the structure and function of the VSD in Ci-VSP.
- Comparison of VSPs with voltage-gated channels (VGCs) regarding voltage sensing.
Main Results:
- Ci-VSP possesses a VSD structurally similar to those in VGCs.
- Ci-VSP generates sensing currents in response to voltage changes.
- Unlike VGCs, VSPs are monomeric and their catalytic domains can be separated from the VSD.
Conclusions:
- VSPs serve as excellent models for studying isolated VSD activity.
- Understanding VSPs advances knowledge of how proteins sense membrane potential.
- This review focuses on the electrical, rather than enzymatic, aspects of VSPs.
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