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Tuning the voltage-sensor motion with a single residue.

Jérôme J Lacroix¹, Francisco Bezanilla¹

¹Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, Illinois.

Biophysical Journal

|September 6, 2012

Summary

The voltage-sensitive phosphatase (Ci-VSP) from Ciona intestinalis has a unique voltage sensing mechanism. Residue I126 in the S1 segment significantly tunes Ci-VSP activation kinetics and voltage dependence.

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Area of Science:

Biophysics
Molecular Biology
Enzymology

Background:

The Ciona intestinalis voltage-sensitive phosphatase (Ci-VSP) is the first identified enzyme regulated by a voltage-sensor domain (VSD).
Its VSD is related to those in voltage-gated ion channels but exhibits distinct voltage dependence and kinetics.
The precise voltage sensing mechanism of Ci-VSP remains incompletely understood.

Discussion:

This study investigates the role of specific residues in the VSD of Ci-VSP.
It examines how mutations affect VSD movement, voltage dependence, and activation kinetics.
The findings highlight a unique voltage sensing mechanism in Ci-VSP compared to ion channels.

Key Insights:

The conserved isoleucine at position 126 (I126) in the S1 segment critically influences Ci-VSP activation.
Modulating the size of I126 tunes VSD movement kinetics over two orders of magnitude and shifts voltage dependence by over 120 mV.
Mutations of phenylalanine at position 161 (F161) in the S2 segment do not significantly alter VSD voltage dependence, suggesting a unique sensing mechanism.

Outlook:

Further research can elucidate the detailed molecular interactions governing Ci-VSP voltage sensing.
Understanding this unique mechanism could inform the design of novel voltage-controlled biological tools.
Comparative studies with other VSD-containing proteins may reveal broader principles of voltage sensing.