論文

査読有り
2016年11月29日

Erratum: Voltage-dependent motion of the catalytic region of voltage-sensing phosphatase monitored by a fluorescent amino acid (Proceedings of the National Academy of Sciences of the United States of America (2016) 113:27 (7521-7526) DOI: 10.1073/pnas.1604218113)

Proceedings of the National Academy of Sciences of the United States of America
  • Souhei Sakata
  • ,
  • Yuka Jinno
  • ,
  • Akira Kawanabe
  • ,
  • Yasushi Okamura

113
27
開始ページ
7521
終了ページ
7526
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1073/pnas.1604218113
出版者・発行元
National Academy of Sciences

The cytoplasmic region of voltage-sensing phosphatase (VSP) derives the voltage dependence of its catalytic activity from coupling to a voltage sensor homologous to that of voltage-gated ion channels. To assess the conformational changes in the cytoplasmic region upon activation of the voltage sensor, we genetically incorporated a fluorescent unnatural amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), into the catalytic region of Ciona intestinalis VSP (Ci-VSP). Measurements of Anap fluorescence under voltage clamp in Xenopus oocytes revealed that the catalytic region assumes distinct conformations dependent on the degree of voltage-sensor activation. FRET analysis showed that the catalytic region remains situated beneath the plasma membrane, irrespective of the voltage level. Moreover, Anap fluorescence from a membrane-facing loop in the C2 domain showed a pattern reflecting substrate turnover. These results indicate that the voltage sensor regulates Ci-VSP catalytic activity by causing conformational changes in the entire catalytic region, without changing their distance from the plasma membrane.

リンク情報
DOI
https://doi.org/10.1073/pnas.1604218113
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/27330112
ID情報
  • DOI : 10.1073/pnas.1604218113
  • ISSN : 0027-8424
  • ISSN : 1091-6490
  • PubMed ID : 27330112
  • SCOPUS ID : 84976571368

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