Voltage-Sensing Phosphatases: Biophysics, Physiology, and Molecular Engineering.

Abstract:

:Voltage-sensing phosphatase (VSP) contains a voltage sensor domain (VSD) similar to that in voltage-gated ion channels, and a phosphoinositide phosphatase region similar to phosphatase and tensin homolog deleted on chromosome 10 (PTEN). The VSP gene is conserved from unicellular organisms to higher vertebrates. Membrane depolarization induces electrical driven conformational rearrangement in the VSD, which is translated into catalytic enzyme activity. Biophysical and structural characterization has revealed details of the mechanisms underlying the molecular functions of VSP. Coupling between the VSD and the enzyme is tight, such that enzyme activity is tuned in a graded fashion to the membrane voltage. Upon VSP activation, multiple species of phosphoinositides are simultaneously altered, and the profile of enzyme activity depends on the history of the membrane potential. VSPs have been the obvious candidate link between membrane potential and phosphoinositide regulation. However, patterns of voltage change regulating VSP in native cells remain largely unknown. This review addresses the current understanding of the biophysical biochemical properties of VSP and provides new insight into the proposed functions of VSP.

journal_name

Physiol Rev

journal_title

Physiological reviews

authors

Okamura Y,Kawanabe A,Kawai T

doi

10.1152/physrev.00056.2017

subject

Has Abstract

pub_date

2018-10-01 00:00:00

pages

2097-2131

issue

4

eissn

0031-9333

issn

1522-1210

journal_volume

98

pub_type

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