Domain-to-domain coupling in voltage-sensing phosphatase

• Sakata Souhei

  Department of Physiology, Division of Life Sciences, Faculty of Medicine, Osaka Medical College

• Matsuda Makoto

  Laboratory of Integrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University Present address: Institute for Protein Research, Osaka University

• Kawanabe Akira

  Laboratory of Integrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University

• Okamura Yasushi

  Laboratory of Integrative Physiology, Department of Physiology, Graduate School of Medicine, Osaka University Graduate School of Frontier Bioscience, Osaka University

Abstract

Voltage-sensing phosphatase (VSP) consists of a transmembrane voltage sensor and a cytoplasmic enzyme region. The enzyme region contains the phosphatase and C2 domains, is structurally similar to the tumor suppressor phosphatase PTEN, and catalyzes the dephosphorylation of phosphoinositides. The transmembrane voltage sensor is connected to the phosphatase through a short linker region, and phosphatase activity is induced upon membrane depolarization. Although the detailed molecular characteristics of the voltage sensor domain and the enzyme region have been revealed, little is known how these two regions are coupled. In addition, it is important to know whether mechanism for coupling between the voltage sensor domain and downstream effector function is shared among other voltage sensor domain-containing proteins. Recent studies in which specific amino acid sites were genetically labeled using a fluorescent unnatural amino acid have enabled detection of the local structural changes in the cytoplasmic region of Ciona intestinalis VSP that occur with a change in membrane potential. The results of those studies provide novel insight into how the enzyme activity of the cytoplasmic region of VSP is regulated by the voltage sensor domain.

Journal

• Biophysics and Physicobiology

  Biophysics and Physicobiology 14 (0), 85-97, 2017

  The Biophysical Society of Japan

Keywords

• membrane potential
• phosphoinositide
• ion channel

Details

• CRID: 1390282680740849024
• NII Article ID: 130007041363
• DOI: 10.2142/biophysico.14.0_85
• ISSN: 21894779
• Web Site: https://www.jstage.jst.go.jp/article/biophysico/14/0/14_85/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed