TY - JOUR
T1 - Mechanosensitivity of ion channels based on protein-lipid interactions
AU - Yoshimura, Kenjiro
AU - Sokabe, Masahiro
PY - 2010/6/6
Y1 - 2010/6/6
N2 - Ion channels forma group ofmembrane 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.
AB - Ion channels forma group ofmembrane 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.
KW - Ion channels
KW - Mechanosensitive channel of large conductance
KW - Mechanosensitive channel of small conductance
KW - Mechanosensitive channels
KW - Membrane lipid
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U2 - 10.1098/rsif.2010.0095.focus
DO - 10.1098/rsif.2010.0095.focus
M3 - Review article
C2 - 20356872
AN - SCOPUS:77956906517
SN - 1742-5689
VL - 7
SP - S307-S320
JO - Journal of the Royal Society Interface
JF - Journal of the Royal Society Interface
IS - SUPPL. 3
ER -