Mechanistic basis for the recognition of laminin-511 by α6β1 integrin

Takizawa, Mamoru; Arimori, Takao; Taniguchi, Yukimasa; Kitago, Yu; Yamashita, Erika; Takagi, Junichi; Sekiguchi, Kiyotoshi

doi:https://doi.org/10.1126/sciadv.1701497

Mechanistic basis for the recognition of laminin-511 by α6β1 integrin

Takizawa, Mamoru; Arimori, Takao; Taniguchi, Yukimasa et al.

Science Advances, 2017, 3(9), e1701497

Number of Access:787（2025-07-06 20:04 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71808

Link to primary information

File	Format	Terms of use	Size	Views	Date.Available	Description	information
SciAdv_e1701497	pdf	None	1.19 MB	298	2019.05.07

Creative Commons : Attribution - NonCommercial

Item Information

Output File Export EndNote Basic Export Mendeley

Title	Mechanistic basis for the recognition of laminin-511 by α6β1 integrin
Creator	CreatorName Takizawa, Mamoru
	NRID 1000080582064 1000080582064 researchmap permalink t_arimori t_arimori Scopus Author ID 35336011300 35336011300 CreatorName Arimori, Takao
	CreatorName Taniguchi, Yukimasa
	NRID 1000060507185 1000060507185 CreatorName Kitago, Yu
	CreatorName Yamashita, Erika
	NRID 1000090212000 1000090212000 researchmap permalink read0105692 read0105692 Scopus Author ID 7102173538 7102173538 CreatorName Takagi, Junichi
	NRID 1000050187845 1000050187845 researchmap permalink read0054833 read0054833 Scopus Author ID 7201662709 7201662709 ORCID 0000-0002-6433-1410 0000-0002-6433-1410 CreatorName Sekiguchi, Kiyotoshi
Description	Mamoru Takizawa, Takao Arimori, Yukimasa Taniguchi, Yu Kitago, Erika Yamashita, Junichi Takagi and Kiyotoshi Sekiguchi, "Mechanistic basis for the recognition of laminin-511 by α6β1 integrin", Science Advances, Vol. 3, No. 9, e1701497, AAAS, 2017
Abstract	Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins—three laminin globular domains of the α chain (LG1–3) and the carboxyl-terminal tail of the γ chain (γ-tail)—are required for integrin binding, but it remains unclear how the γ-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the γ-tail extends to the bottom face of LG1–3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1–3 with the γ1-tail apposed to the metal ion–dependent adhesion site (MIDAS) of integrin β1. These findings are consistent with a model in which the γ-tail coordinates the metal ion in the MIDAS through its Glu residue.
Publisher	American Association for the Advancement of Science
Source Title	Science Advances
Volume (Issue)	3(9)
Page	e1701497
Date of Issued	2017-09
Language	English
Handle URL	https://hdl.handle.net/11094/71808
eISSN	23752548
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1126/sciadv.1701497
Access Rights	open access
CopyRight	© 2017 The Authors. This article is licensed under a Creative Commons Attribution-NonCommercial 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	Science Advances. 2017, 3(9), p. e1701497
DC.title	Mechanistic basis for the recognition of laminin-511 by α6β1 integrin
DC.creator	Takizawa, Mamoru
	Arimori, Takao
	Taniguchi, Yukimasa
	Kitago, Yu
	Yamashita, Erika
	Takagi, Junichi
	Sekiguchi, Kiyotoshi
DC.publisher	American Association for the Advancement of Science
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2017-09
DC.identifier	https://doi.org/10.1126/sciadv.1701497
DC.description	Mamoru Takizawa, Takao Arimori, Yukimasa Taniguchi, Yu Kitago, Erika Yamashita, Junichi Takagi and Kiyotoshi Sekiguchi, "Mechanistic basis for the recognition of laminin-511 by α6β1 integrin", Science Advances, Vol. 3, No. 9, e1701497, AAAS, 2017
DCTERMS.abstract	Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins—three laminin globular domains of the α chain (LG1–3) and the carboxyl-terminal tail of the γ chain (γ-tail)—are required for integrin binding, but it remains unclear how the γ-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the γ-tail extends to the bottom face of LG1–3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1–3 with the γ1-tail apposed to the metal ion–dependent adhesion site (MIDAS) of integrin β1. These findings are consistent with a model in which the γ-tail coordinates the metal ion in the MIDAS through its Glu residue.
DC.rights	© 2017 The Authors. This article is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
DC.format	71808
citation_title	Mechanistic basis for the recognition of laminin-511 by α6β1 integrin
citation_author	Takizawa, Mamoru
	Arimori, Takao
	Taniguchi, Yukimasa
	Kitago, Yu
	Yamashita, Erika
	Takagi, Junichi
	Sekiguchi, Kiyotoshi
citation_publisher	American Association for the Advancement of Science
citation_language	English
citation_date	2017-09
citation_journal_title	Science Advances
citation_volume	3
citation_issue	9
citation_firstpage	e1701497
citation_doi	https://doi.org/10.1126/sciadv.1701497
citation_public_url	https://hdl.handle.net/11094/71808

Mechanistic basis for the recognition of laminin-511 by α6β1 integrin

Link to primary information

Item Information

Show details