2010年6月
Mechanosensitivity of ion channels based on protein-lipid interactions
JOURNAL OF THE ROYAL SOCIETY INTERFACE
- ,
- 巻
- 7
- 号
- 開始ページ
- S307
- 終了ページ
- S320
- 記述言語
- 英語
- 掲載種別
- 書評論文,書評,文献紹介等
- DOI
- 10.1098/rsif.2010.0095.focus
- 出版者・発行元
- ROYAL SOC
Ion channels forma group of membrane proteins that pass ions through a pore beyond the energy barrier of the lipid bilayer. The structure of the transmembrane segment of membrane proteins is influenced by the charges and the hydrophobicity of the surrounding lipids and the pressure on its surface. A mechanosensitive channel is specifically designed to change its conformation in response to changes in the membrane pressure (tension). However, mechanosensitive channels are not the only group that is sensitive to the physical environment of the membrane: voltage-gated channels are also amenable to the lipid environment. In this article, we review the structure and gating mechanisms of the mechanosensitive channels and voltage-gated channels and discuss how their functions are affected by the physical properties of the lipid bilayer.
- リンク情報
- ID情報
-
- DOI : 10.1098/rsif.2010.0095.focus
- ISSN : 1742-5689
- Web of Science ID : WOS:000280131400003