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

Inanobe, Atsushi; Nakagawa, Atushi; Matsuura, Takanori; Kurachi, Yoshihisa

doi:https://doi.org/10.1074/jbc.M110.161703

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

アクセス数:1,622件（2025-04-27 02:19 集計）

固定URL: https://hdl.handle.net/11094/73656

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タイトル	A structural determinant for the control of PIP_2 sensitivity in G protein-gated inward rectifier K^+ channels
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
	著者名 Matsuura, Takanori
	NRID 1000030142011 1000030142011 著者名 Kurachi, Yoshihisa
内容	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.
抄録	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.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	285(49)
ページ	38517-38523
刊行年月	2010-12
言語	英語
ハンドルURL	https://hdl.handle.net/11094/73656
eISSN	1083351X
NCID	AA1202441X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M110.161703
関連情報 (isIdenticalTo)	PMID 20880843
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

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2010, 285(49), p. 38517-38523
DC.title	A structural determinant for the control of PIP_2 sensitivity in G protein-gated inward rectifier K^+ channels
DC.creator	Inanobe, Atsushi
	Nakagawa, Atushi
	Matsuura, Takanori
	Kurachi, Yoshihisa
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2010-12
DC.identifier	https://doi.org/10.1074/jbc.M110.161703
DC.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.
DCTERMS.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.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
DC.format	73656
citation_title	A structural determinant for the control of PIP_2 sensitivity in G protein-gated inward rectifier K^+ channels
citation_author	Inanobe, Atsushi
	Nakagawa, Atushi
	Matsuura, Takanori
	Kurachi, Yoshihisa
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2010-12
citation_journal_title	Journal of Biological Chemistry
citation_volume	285
citation_issue	49
citation_firstpage	38517
citation_lastpage	38523
citation_doi	https://doi.org/10.1074/jbc.M110.161703
citation_pmid	20880843
citation_public_url	https://hdl.handle.net/11094/73656

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

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