Structural basis for the membrane association of ankyrinG via palmitoylation

Fujiwara, Yuichiro; Kondo, Hiroko X.; Shirota, Matsuyuki; Kobayashi, Megumi; Takeshita, Kohei; Nakagawa, Atushi; Okamura, Yasushi; Kinoshita, Kengo

doi:https://doi.org/10.1038/srep23981

Structural basis for the membrane association of ankyrinG via palmitoylation

Fujiwara, Yuichiro; Kondo, Hiroko X.; Shirota, Matsuyuki et al.

Scientific Reports, 2016, 6, 23981

Number of Access:1,043（2025-07-18 09:53 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73667

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Title	Structural basis for the membrane association of ankyrinG via palmitoylation
Creator	NRID 1000020532980 1000020532980 CreatorName Fujiwara, Yuichiro
	CreatorName Kondo, Hiroko X.
	NRID 1000000549462 1000000549462 CreatorName Shirota, Matsuyuki
	CreatorName Kobayashi, Megumi
	NRID 1000080346808 1000080346808 CreatorName Takeshita, Kohei
	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
	NRID 1000080201987 1000080201987 researchmap permalink yasushiokamura yasushiokamura Scopus Author ID 55322083200 55322083200 ORCID 0000-0001-5386-7968 0000-0001-5386-7968 CreatorName Okamura, Yasushi
	NRID 1000060332293 1000060332293 CreatorName Kinoshita, Kengo
Description	Fujiwara, Y., Kondo, H., Shirota, M. et al. Structural basis for the membrane association of ankyrinG via palmitoylation. Sci Rep 6, 23981 (2016) doi:10.1038/srep23981
Abstract	By clustering various ion channels and transporters, ankyrin-G (AnkG) configures the membraneexcitation platforms in neurons and cardiomyocytes. AnkG itself localizes to specific areas on the plasma membrane via s-palmitoylation of Cys. However, the structural mechanism by which AnkG anchors to the membrane is not understood. In this study, we solved the crystal structures of the reduced and oxidized forms of the AnkG s-palmitoylation domain and used multiple long-term coarsegrained molecular dynamics simulations to analyze their membrane association. Here we report that the membrane anchoring of AnkG was facilitated by s-palmitoylation, defining a stable binding interface on the lipid membrane, and that AnkG without s-palmitoylation also preferred to stay near the membrane but did not have a unique binding interface. This suggests that AnkG in the juxtamembrane region is primed to accept lipid modification at Cys, and once that happens AnkG constitutes a rigid structural base upon which a membrane-excitation platform can be assembled.
Publisher	Springer Nature
Source Title	Scientific Reports
Volume (Issue)	6
Page	23981
Date of Issued	2016-04
Language	English
Handle URL	https://hdl.handle.net/11094/73667
eISSN	20452322
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1038/srep23981
Relation.isIdenticalTo	PMID 27046665
Access Rights	open access
CopyRight	© 2016 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Scientific Reports. 2016, 6, p. 23981
DC.title	Structural basis for the membrane association of ankyrinG via palmitoylation
DC.creator	Fujiwara, Yuichiro
	Kondo, Hiroko X.
	Shirota, Matsuyuki
	Kobayashi, Megumi
	Takeshita, Kohei
	Nakagawa, Atushi
	Okamura, Yasushi
	Kinoshita, Kengo
DC.publisher	Springer Nature
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2016-04
DC.identifier	https://doi.org/10.1038/srep23981
DC.description	Fujiwara, Y., Kondo, H., Shirota, M. et al. Structural basis for the membrane association of ankyrinG via palmitoylation. Sci Rep 6, 23981 (2016) doi:10.1038/srep23981
DCTERMS.abstract	By clustering various ion channels and transporters, ankyrin-G (AnkG) configures the membraneexcitation platforms in neurons and cardiomyocytes. AnkG itself localizes to specific areas on the plasma membrane via s-palmitoylation of Cys. However, the structural mechanism by which AnkG anchors to the membrane is not understood. In this study, we solved the crystal structures of the reduced and oxidized forms of the AnkG s-palmitoylation domain and used multiple long-term coarsegrained molecular dynamics simulations to analyze their membrane association. Here we report that the membrane anchoring of AnkG was facilitated by s-palmitoylation, defining a stable binding interface on the lipid membrane, and that AnkG without s-palmitoylation also preferred to stay near the membrane but did not have a unique binding interface. This suggests that AnkG in the juxtamembrane region is primed to accept lipid modification at Cys, and once that happens AnkG constitutes a rigid structural base upon which a membrane-excitation platform can be assembled.
DC.rights	© 2016 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	73667
citation_title	Structural basis for the membrane association of ankyrinG via palmitoylation
citation_author	Fujiwara, Yuichiro
	Kondo, Hiroko X.
	Shirota, Matsuyuki
	Kobayashi, Megumi
	Takeshita, Kohei
	Nakagawa, Atushi
	Okamura, Yasushi
	Kinoshita, Kengo
citation_publisher	Springer Nature
citation_language	English
citation_date	2016-04
citation_journal_title	Scientific Reports
citation_volume	6
citation_firstpage	23981
citation_doi	https://doi.org/10.1038/srep23981
citation_pmid	27046665
citation_public_url	https://hdl.handle.net/11094/73667

Structural basis for the membrane association of ankyrinG via palmitoylation

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