Cargando…

Domain-to-domain coupling in voltage-sensing phosphatase

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 tra...

Descripción completa

Detalles Bibliográficos
Autores principales: Sakata, Souhei, Matsuda, Makoto, Kawanabe, Akira, Okamura, Yasushi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Biophysical Society of Japan (BSJ) 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5515349/
https://www.ncbi.nlm.nih.gov/pubmed/28744425
http://dx.doi.org/10.2142/biophysico.14.0_85
_version_ 1783250979991322624
author Sakata, Souhei
Matsuda, Makoto
Kawanabe, Akira
Okamura, Yasushi
author_facet Sakata, Souhei
Matsuda, Makoto
Kawanabe, Akira
Okamura, Yasushi
author_sort Sakata, Souhei
collection PubMed
description 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.
format Online
Article
Text
id pubmed-5515349
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher The Biophysical Society of Japan (BSJ)
record_format MEDLINE/PubMed
spelling pubmed-55153492017-07-25 Domain-to-domain coupling in voltage-sensing phosphatase Sakata, Souhei Matsuda, Makoto Kawanabe, Akira Okamura, Yasushi Biophys Physicobiol Review Article 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. The Biophysical Society of Japan (BSJ) 2017-06-23 /pmc/articles/PMC5515349/ /pubmed/28744425 http://dx.doi.org/10.2142/biophysico.14.0_85 Text en 2017 © The Biophysical Society of Japan
spellingShingle Review Article
Sakata, Souhei
Matsuda, Makoto
Kawanabe, Akira
Okamura, Yasushi
Domain-to-domain coupling in voltage-sensing phosphatase
title Domain-to-domain coupling in voltage-sensing phosphatase
title_full Domain-to-domain coupling in voltage-sensing phosphatase
title_fullStr Domain-to-domain coupling in voltage-sensing phosphatase
title_full_unstemmed Domain-to-domain coupling in voltage-sensing phosphatase
title_short Domain-to-domain coupling in voltage-sensing phosphatase
title_sort domain-to-domain coupling in voltage-sensing phosphatase
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5515349/
https://www.ncbi.nlm.nih.gov/pubmed/28744425
http://dx.doi.org/10.2142/biophysico.14.0_85
work_keys_str_mv AT sakatasouhei domaintodomaincouplinginvoltagesensingphosphatase
AT matsudamakoto domaintodomaincouplinginvoltagesensingphosphatase
AT kawanabeakira domaintodomaincouplinginvoltagesensingphosphatase
AT okamurayasushi domaintodomaincouplinginvoltagesensingphosphatase