Interactions of Cations with the Cytoplasmic Pores of Inward Rectifier K^+ Channels in the Closed State

Inanobe, Atsushi; Nakagawa, Atushi; Kurachi, Yoshihisa

Journal of Biological Chemistry, 2011, 286(48), 41801-41811

アクセス数:198件（2025-04-27 01:42 集計）

固定URL: https://hdl.handle.net/11094/73660

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タイトル
Interactions of Cations with the Cytoplasmic Pores of Inward Rectifier K^+ Channels in the Closed State
著者
NRID
1000000270851 1000000270851
researchmap permalink
read0051668 read0051668
Scopus Author ID
7004862161 7004862161
著者名
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
著者名
Nakagawa, Atushi
NRID
1000030142011 1000030142011
著者名
Kurachi, Yoshihisa
内容
This research was originally published in Journal of Biological Chemistry. Atsushi Inanobe, Atsushi Nakagawa, and Yoshihisa Kurachi. Interactions of Cations with the Cytoplasmic Pores of Inward Rectifier K^+ Channels in the Closed State. Journal of Biological Chemistry. 2011; 286, 41801-41811. © the American Society for Biochemistry and Molecular Biology.
抄録
Ion channels gate at membrane-embedded domains by changing their conformation along the ion conduction pathway. Inward rectifier K^＋ (Kir) channels possess a unique extramembrane cytoplasmic domain that extends this pathway. However, the relevance and contribution of this domain to ion permeation remain unclear. By qualitative x-ray crystallographic analysis, we found that the pore in the cytoplasmic domain of Kir3.2 binds cations in a valency-dependent manner and does not allow the displacement of Mg^<2＋> by monovalent cations or spermine. Electrophysiological analyses revealed that the cytoplasmic pore of Kir3.2 selectively binds positively charged molecules and has a higher affinity for Mg^<2＋> when it has a low probability of being open. The selective blocking of chemical modification of the side chain of pore-facing residues byMg^<2＋> indicates that the mode of binding of Mg^<2＋> is likely to be similar to that observed in the crystal structure. These results indicate that the Kir3.2 crystal structure has a closed conformation with a negative electrostatic field potential at the cytoplasmic pore, the potential of which may be controlled by conformational changes in the cytoplasmic domain to regulate ion diffusion along the pore.
出版者
American Society for Biochemistry and Molecular Biology
収録物名
Journal of Biological Chemistry
巻(号)
286(48)
ページ
41801-41811
刊行年月
2011-12
言語
英語
ハンドルURL
https://hdl.handle.net/11094/73660
eISSN
1083351X
NCID
AA1202441X
関連情報 (isIdenticalTo)
DOI (出版社版)
https://doi.org/10.1074/jbc.M111.278531
PMID
21982822
アクセス権
open access
権利情報
© the American Society for Biochemistry and Molecular Biology.
出版タイプ
Version of Record
カテゴリ
学術雑誌論文 Journal Article