論文

査読有り 国際誌
2022年6月28日

Interaction between S4 and the phosphatase domain mediates electrochemical coupling in voltage-sensing phosphatase (VSP).

Proceedings of the National Academy of Sciences of the United States of America
  • Natsuki Mizutani
  • ,
  • Akira Kawanabe
  • ,
  • Yuka Jinno
  • ,
  • Hirotaka Narita
  • ,
  • Tomoko Yonezawa
  • ,
  • Atsushi Nakagawa
  • ,
  • Yasushi Okamura

119
26
開始ページ
e2200364119
終了ページ
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1073/pnas.2200364119

Voltage-sensing phosphatase (VSP) consists of a voltage sensor domain (VSD) and a cytoplasmic catalytic region (CCR), which is similar to phosphatase and tensin homolog (PTEN). How the VSD regulates the innate enzyme component of VSP remains unclear. Here, we took a combined approach that entailed the use of electrophysiology, fluorometry, and structural modeling to study the electrochemical coupling in Ciona intestinalis VSP. We found that two hydrophobic residues at the lowest part of S4 play an essential role in the later transition of VSD-CCR coupling. Voltage clamp fluorometry and disulfide bond locking indicated that S4 and its neighboring linker move as one helix (S4-linker helix) and approach the hydrophobic spine in the CCR, a structure located near the cell membrane and also conserved in PTEN. We propose that the hydrophobic spine operates as a hub for translating an electrical signal into a chemical one in VSP.

リンク情報
DOI
https://doi.org/10.1073/pnas.2200364119
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/35733115
ID情報
  • DOI : 10.1073/pnas.2200364119
  • PubMed ID : 35733115

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