The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins

Ido, Hiroyuki; Nakamura, Aya; Kobayashi, Reiko; Ito, Shunsuke; Li, Shaoliang; Futaki, Sugiko; Sekiguchi, Kiyotoshi

doi:https://doi.org/10.1074/jbc.M609402200

The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins

Ido, Hiroyuki; Nakamura, Aya; Kobayashi, Reiko et al.

Journal of Biological Chemistry, 2007, 282(15), 11144-11154

Number of Access:975（2025-08-18 12:31 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71428

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Title	The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins
Creator	CreatorName Ido, Hiroyuki
	CreatorName Nakamura, Aya
	CreatorName Kobayashi, Reiko
	CreatorName Ito, Shunsuke
	NRID 1000040252720 1000040252720 CreatorName Li, Shaoliang
	NRID 1000000403014 1000000403014 CreatorName Futaki, Sugiko
	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	This research was originally published in the Journal of Biological Chemistry. Hiroyuki Ido, Aya Nakamura, Reiko Kobayashi, Shunsuke Ito, Shaoliang Li, Sugiko Futaki and Kiyotoshi Sekiguchi. The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins. J. Biol. Chem. 2007; 282: 11144–11154 © the American Society for Biochemistry and Molecular Biology
Abstract	Laminins are the major cell-adhesive proteins in the basement membrane, consisting of three subunits termed α, β, and γ. The putative binding site for integrins has been mapped to the G domain of the α chain, although trimerization with β and γ chains is necessary for the G domain to exert its integrin binding activity. The mechanism underlying the requirement of β and γ chains in integrin binding by laminins remains poorly understood. Here, we show that the C-terminal region of the γ chain is involved in modulation of the integrin binding activity of laminins. We found that deletion of the C-terminal three but not two amino acids within the γ1 chain completely abrogated the integrin binding activity of laminin-511. Furthermore, substitution of Gln for Glu-1607, the amino acid residue at the third position from the C terminus of the γ1 chain, also abolished the integrin binding activity, underscoring the role of Glu-1607 in integrin binding by the laminin. We also found that the conserved Glu residue of the γ2 chain is necessary for integrin binding by laminin-332, suggesting that the same mechanism operates in the modulation of the integrin binding activity of laminins containing either γ1 or γ2 chains. However, the peptide segment modeled after the C-terminal region of γ1 chain was incapable of either binding to integrin or inhibiting integrin binding by laminin-511, making it unlikely that the Glu residue is directly recognized by integrin. These results, together, indicate a novel mechanism operating in ligand recognition by laminin binding integrins.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	282(15)
Page	11144-11154
Date of Issued	2007-04
Language	English
Handle URL	https://hdl.handle.net/11094/71428
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M609402200
Access Rights	open access
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	Journal of Biological Chemistry. 2007, 282(15), p. 11144-11154
DC.title	The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins
DC.creator	Ido, Hiroyuki
	Nakamura, Aya
	Kobayashi, Reiko
	Ito, Shunsuke
	Li, Shaoliang
	Futaki, Sugiko
	Sekiguchi, Kiyotoshi
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2007-04
DC.identifier	https://doi.org/10.1074/jbc.M609402200
DC.description	This research was originally published in the Journal of Biological Chemistry. Hiroyuki Ido, Aya Nakamura, Reiko Kobayashi, Shunsuke Ito, Shaoliang Li, Sugiko Futaki and Kiyotoshi Sekiguchi. The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins. J. Biol. Chem. 2007; 282: 11144–11154 © the American Society for Biochemistry and Molecular Biology
DCTERMS.abstract	Laminins are the major cell-adhesive proteins in the basement membrane, consisting of three subunits termed α, β, and γ. The putative binding site for integrins has been mapped to the G domain of the α chain, although trimerization with β and γ chains is necessary for the G domain to exert its integrin binding activity. The mechanism underlying the requirement of β and γ chains in integrin binding by laminins remains poorly understood. Here, we show that the C-terminal region of the γ chain is involved in modulation of the integrin binding activity of laminins. We found that deletion of the C-terminal three but not two amino acids within the γ1 chain completely abrogated the integrin binding activity of laminin-511. Furthermore, substitution of Gln for Glu-1607, the amino acid residue at the third position from the C terminus of the γ1 chain, also abolished the integrin binding activity, underscoring the role of Glu-1607 in integrin binding by the laminin. We also found that the conserved Glu residue of the γ2 chain is necessary for integrin binding by laminin-332, suggesting that the same mechanism operates in the modulation of the integrin binding activity of laminins containing either γ1 or γ2 chains. However, the peptide segment modeled after the C-terminal region of γ1 chain was incapable of either binding to integrin or inhibiting integrin binding by laminin-511, making it unlikely that the Glu residue is directly recognized by integrin. These results, together, indicate a novel mechanism operating in ligand recognition by laminin binding integrins.
DC.format	71428
citation_title	The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins
citation_author	Ido, Hiroyuki
	Nakamura, Aya
	Kobayashi, Reiko
	Ito, Shunsuke
	Li, Shaoliang
	Futaki, Sugiko
	Sekiguchi, Kiyotoshi
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2007-04
citation_journal_title	Journal of Biological Chemistry
citation_volume	282
citation_issue	15
citation_firstpage	11144
citation_lastpage	11154
citation_doi	https://doi.org/10.1074/jbc.M609402200
citation_public_url	https://hdl.handle.net/11094/71428

The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin γ Chains in Integrin Binding by Laminins

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