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基于蛋白-脂双层相互作用的离子通道的机械敏感性。

Mechanosensitivity of ion channels based on protein-lipid interactions.

机构信息

Department of Biology, University of Maryland, College Park, MD 20742, USA.

出版信息

J R Soc Interface. 2010 Jun 6;7 Suppl 3(Suppl 3):S307-20. doi: 10.1098/rsif.2010.0095.focus. Epub 2010 Mar 31.


DOI:10.1098/rsif.2010.0095.focus
PMID:20356872
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2943882/
Abstract

Ion channels form a 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.

摘要

离子通道是一组膜蛋白,它们通过脂质双层的能量屏障以外的孔道传递离子。膜蛋白跨膜片段的结构受周围脂质的电荷和疏水性以及其表面压力的影响。机械敏感通道专门设计用于响应膜压力(张力)的变化而改变其构象。然而,机械敏感通道并不是唯一对膜物理环境敏感的通道:电压门控通道也能适应脂质环境。在本文中,我们回顾了机械敏感通道和电压门控通道的结构和门控机制,并讨论了它们的功能如何受脂质双层物理性质的影响。

相似文献

[1]
Mechanosensitivity of ion channels based on protein-lipid interactions.

J R Soc Interface. 2010-3-31

[2]
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[3]
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[4]
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[5]
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[6]
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[7]
Hydration properties of mechanosensitive channel pores define the energetics of gating.

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[8]
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[9]
Thermodynamics of mechanosensitivity.

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[10]
Collective response of self-organized clusters of mechanosensitive channels.

Phys Rev E Stat Nonlin Soft Matter Phys. 2011-2

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本文引用的文献

[1]
The tension-transmitting 'clutch' in the mechanosensitive channel MscS.

Nat Struct Mol Biol. 2010-3-7

[2]
Curvature generation and pressure profile modulation in membrane by lysolipids: insights from coarse-grained simulations.

Biophys J. 2009-10-21

[3]
Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy.

Nature. 2009-9-10

[4]
The mechanotransduction machinery of hair cells.

Sci Signal. 2009-8-25

[5]
Structure of a tetrameric MscL in an expanded intermediate state.

Nature. 2009-9-3

[6]
Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening.

Biophys J. 2009-8-19

[7]
Crystal structure of the ATP-gated P2X(4) ion channel in the closed state.

Nature. 2009-7-30

[8]
Three-dimensional structure of CaV3.1: comparison with the cardiac L-type voltage-gated calcium channel monomer architecture.

J Biol Chem. 2009-8-14

[9]
Structure of the connexin 26 gap junction channel at 3.5 A resolution.

Nature. 2009-4-2

[10]
An open-pore structure of the mechanosensitive channel MscL derived by determining transmembrane domain interactions upon gating.

FASEB J. 2009-7

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