Regulation of TRP channels: A voltage-lipid connection

B. Nilius, F. Mahieu, Y. Karashima, T. Voets

研究成果: ジャーナルへの寄稿学術誌査読

56 被引用数 (Scopus)

抄録

TRP (transient receptor potential) channels respond to a plethora of stimuli in a fine-tuned manner. We show here that both membrane potential and the level of PI (phosphatidylinositol) phosphates are efficient regulators of TRP channel gating. Recent work has shown that this regulation applies to several members of the TRPV (TRP vanilloid) subfamily (TRPV1 and TRPV5) and the TRPM (TRP melastatin) subfamily (TRPM4/ TRPM5/TRPM7/TRPM8), whereas regulation of members of the TRPC subfamily is still disputed. The mechanism whereby PIP2 (PI 4,5-bisphosphate) acts on TRPM4, a Ca2+- and voltage-activated channel, is shown in detail in this paper: (i) PIP2 may bind directly to the channel, (ii) PIP2 induces sensitization to activation by Ca2+, and (iii) PIP2 shifts the voltage dependence towards negative and physiologically more meaningful potentials. A PIP2-binding pocket seems to comprise a part of the TRP domain and especially pleckstrin homology domains in the C-terminus.

本文言語英語
ページ(範囲)105-108
ページ数4
ジャーナルBiochemical Society Transactions
35
1
DOI
出版ステータス出版済み - 2月 2007
外部発表はい

!!!All Science Journal Classification (ASJC) codes

  • 生化学

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