A structural determinant for the control of PIP_2 sensitivity in G protein-gated inward rectifier K^+ channels

Inanobe, Atsushi; Nakagawa, Atushi; Matsuura, Takanori et al.

Journal of Biological Chemistry, 2010, 285(49), 38517-38523

Number of Access:2,173（2025-08-14 15:05 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73656

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Title
A structural determinant for the control of PIP_2 sensitivity in G protein-gated inward rectifier K^+ channels
Creator
NRID
1000000270851 1000000270851
researchmap permalink
read0051668 read0051668
Scopus Author ID
7004862161 7004862161
CreatorName
Inanobe, Atsushi
NRID
1000020188890 1000020188890
ORCID
0000-0002-1700-7861 0000-0002-1700-7861
researchmap permalink
atsushi_nakagawa atsushi_nakagawa
Scopus Author ID
7202934909 7202934909
CreatorName
Nakagawa, Atushi
CreatorName
Matsuura, Takanori
NRID
1000030142011 1000030142011
CreatorName
Kurachi, Yoshihisa
Description
This research was originally published in Journal of Biological Chemistry. Atsushi Inanobe, Atsushi Nakagawa, Takanori Matsuura and Yoshihisa Kurachi. A structural determinant for the control of PIP2 sensitivity in G protein-gated inward rectifier K^+ channels. Journal of Biological Chemistry. 2010; 285, 38517-38523. © the American Society for Biochemistry and Molecular Biology.
Abstract
Inward rectifier K^+ (Kir) channels are activated by phosphatidylinositol-( 4,5)-bisphosphate (PIP_2), but G protein-gated Kir (K_G) channels further require either G protein βγ subunits (Gβγ) or intracellular Na^+ for their activation. To reveal the mechanism(s) underlying this regulation, we compared the crystal structures of the cytoplasmic domain of K_G channel subunit Kir3.2 obtained in the presence and the absence of Na^+. The Na^+ -free Kir3.2, but not the Na^+ -plus Kir3.2, possessed an ionic bond connecting the N terminus and the CD loop of the C terminus. Functional analyses revealed that the ionic bond between His-69 on theNterminus and Asp-228 on the CD loop, which are known to be critically involved in Gβγ- and Na^+ -dependent activation, lowered PIP_2 sensitivity. The conservation of these residues within the K_G channel family indicates that the ionic bond is a character that maintains the channels in a closed state by controlling the PIP_2 sensitivity.
Publisher
American Society for Biochemistry and Molecular Biology
Source Title
Journal of Biological Chemistry
Volume (Issue)
285(49)
Page
38517-38523
Date of Issued
2010-12
Language
English
Handle URL
https://hdl.handle.net/11094/73656
eISSN
1083351X
NCID
AA1202441X
Relation.isIdenticalTo
DOI (Publisher Version)
https://doi.org/10.1074/jbc.M110.161703
PMID
20880843
Access Rights
open access
CopyRight
© the American Society for Biochemistry and Molecular Biology.
oaire:version
Version of Record
Category
学術雑誌論文 Journal Article