2014年3月
Long alpha helices projecting from the membrane as the dimer interface in the voltage-gated H+ channel
JOURNAL OF GENERAL PHYSIOLOGY
- ,
- ,
- 巻
- 143
- 号
- 3
- 開始ページ
- 377
- 終了ページ
- 386
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1085/jgp.201311082
- 出版者・発行元
- ROCKEFELLER UNIV PRESS
The voltage-gated H+ channel (Hv) is a H+-permeable voltage-sensor domain (VSD) protein that consists of four transmembrane segments (S1-S4). Hv assembles as a dimeric channel and two transmembrane channel domains function cooperatively, which is mediated by the coiled-coil assembly domain in the cytoplasmic C terminus. However, the structural basis of the interdomain interactions remains unknown. Here, we provide a picture of the dimer configuration based on the analyses of interactions among two VSDs and a coiled-coil domain. Systematic mutations of the linker region between S4 of VSD and the coiled-coil showed that the channel gating was altered in the helical periodicity with the linker length, suggesting that two domains are linked by helices. Cross-linking analyses revealed that the two S4 helices were situated closely in the dimeric channel. The interaction interface between the two S4 and the assembly interface of the coiled-coil domain were aligned in the same direction based on the phase angle calculation along alpha helices. Collectively, we propose that continuous helices stretching from the transmembrane to the cytoplasmic region in the dimeric interface regulate the channel activation in the Hv dimer.
- リンク情報
- ID情報
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- DOI : 10.1085/jgp.201311082
- ISSN : 0022-1295
- eISSN : 1540-7748
- Web of Science ID : WOS:000332028700007