Structural insights into tetraspanin CD9 function

Umeda, Rie; Satouh, Yuhkoh; Takemoto, Mizuki; Nakada, Yoshiko; Liu, Kehong; Yokoyama, Takeshi; Shirouzu, Mikako; Iwata, So; Nomura, Norimichi; Sato, Ken; Ikawa, Masahito; Nishizawa, Tomohiro; Nureki, Osamu

doi:https://doi.org/10.1038/s41467-020-15459-7

Structural insights into tetraspanin CD9 function

Umeda, Rie; Satouh, Yuhkoh; Takemoto, Mizuki et al.

Nature Communications, 2020, 11(1), 1606

Number of Access:1,161（2025-08-22 01:04 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/78539

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Title	Structural insights into tetraspanin CD9 function
Creator	CreatorName Umeda, Rie
	NRID 1000040545571 1000040545571 CreatorName Satouh, Yuhkoh
	CreatorName Takemoto, Mizuki
	NRID 1000070799220 1000070799220 CreatorName Nakada, Yoshiko Creator.Alternative Nakura, Yoshiko
	CreatorName Liu, Kehong
	NRID 1000020719447 1000020719447 CreatorName Yokoyama, Takeshi
	NRID 1000070280732 1000070280732 CreatorName Shirouzu, Mikako
	NRID 1000060452330 1000060452330 CreatorName Iwata, So
	NRID 1000010314246 1000010314246 CreatorName Nomura, Norimichi
	NRID 1000030311343 1000030311343 CreatorName Sato, Ken
	NRID 1000020304066 1000020304066 ORCID 0000-0001-9859-6217 0000-0001-9859-6217 researchmap permalink read0054910 read0054910 Scopus Author ID 16689054500 16689054500 CreatorName Ikawa, Masahito
	NRID 1000080599077 1000080599077 CreatorName Nishizawa, Tomohiro
	CreatorName Nureki, Osamu
Description	Umeda, R., Satouh, Y., Takemoto, M. et al. Structural insights into tetraspanin CD9 function. Nat Commun 11, 1606 (2020). https://doi.org/10.1038/s41467-020-15459-7
Abstract	Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exert cellular functions. Here we report the crystal structure of CD9 and the cryo-electron microscopic structure of CD9 in complex with its single membrane-spanning partner protein, EWI-2. The reversed cone-like molecular shape of CD9 generates membrane curvature in the crystalline lipid layers, which explains the CD9 localization in regions with high membrane curvature and its implications in membrane remodeling. The molecular interaction between CD9 and EWI-2 is mainly mediated through the small residues in the transmembrane region and protein/lipid interactions, whereas the fertilization assay revealed the critical involvement of the LEL region in the sperm-egg fusion, indicating the different dependency of each binding domain for other partner proteins.
Publisher	Nature Research
Source Title	Nature Communications
Volume (Issue)	11(1)
Page	1606
Date of Issued	2020-03-20
Language	English
Handle URL	https://hdl.handle.net/11094/78539
eISSN	20411723
NCID	AA12645905
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1038/s41467-020-15459-7
Relation.isIdenticalTo	PMID 32231207
Access Rights	open access
CopyRight	© 2020 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
DCTERMS.bibliographicCitation	Nature Communications. 2020, 11(1), p. 1606
DC.title	Structural insights into tetraspanin CD9 function
DC.creator	Umeda, Rie
	Satouh, Yuhkoh
	Takemoto, Mizuki
	Nakada, Yoshiko
	Liu, Kehong
	Yokoyama, Takeshi
	Shirouzu, Mikako
	Iwata, So
	Nomura, Norimichi
	Sato, Ken
	Ikawa, Masahito
	Nishizawa, Tomohiro
	Nureki, Osamu
DC.creator	Nakura, Yoshiko
DC.publisher	Nature Research
DC.language' scheme='DCTERMS.RFC1766	English
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2020-03-20
DC.identifier	https://doi.org/10.1038/s41467-020-15459-7
DC.description	Umeda, R., Satouh, Y., Takemoto, M. et al. Structural insights into tetraspanin CD9 function. Nat Commun 11, 1606 (2020). https://doi.org/10.1038/s41467-020-15459-7
DCTERMS.abstract	Tetraspanins play critical roles in various physiological processes, ranging from cell adhesion to virus infection. The members of the tetraspanin family have four membrane-spanning domains and short and large extracellular loops, and associate with a broad range of other functional proteins to exert cellular functions. Here we report the crystal structure of CD9 and the cryo-electron microscopic structure of CD9 in complex with its single membrane-spanning partner protein, EWI-2. The reversed cone-like molecular shape of CD9 generates membrane curvature in the crystalline lipid layers, which explains the CD9 localization in regions with high membrane curvature and its implications in membrane remodeling. The molecular interaction between CD9 and EWI-2 is mainly mediated through the small residues in the transmembrane region and protein/lipid interactions, whereas the fertilization assay revealed the critical involvement of the LEL region in the sperm-egg fusion, indicating the different dependency of each binding domain for other partner proteins.
DC.rights	© 2020 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License.
DC.format	78539
citation_title	Structural insights into tetraspanin CD9 function
citation_author	Umeda, Rie
	Satouh, Yuhkoh
	Takemoto, Mizuki
	Nakada, Yoshiko
	Liu, Kehong
	Yokoyama, Takeshi
	Shirouzu, Mikako
	Iwata, So
	Nomura, Norimichi
	Sato, Ken
	Ikawa, Masahito
	Nishizawa, Tomohiro
	Nureki, Osamu
citation_publisher	Nature Research
citation_language	English
citation_date	2020-03-20
citation_journal_title	Nature Communications
citation_volume	11
citation_issue	1
citation_firstpage	1606
citation_doi	https://doi.org/10.1038/s41467-020-15459-7
citation_pmid	32231207
citation_public_url	https://hdl.handle.net/11094/78539

Structural insights into tetraspanin CD9 function

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