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:info:doi/10.1074/jbc.M609402200

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論文情報

タイトル	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
著者	Ido, Hiroyuki Ido, Hiroyuki
	Nakamura, Aya Nakamura, Aya
	Kobayashi, Reiko Kobayashi, Reiko
	Ito, Shunsuke Ito, Shunsuke
	Li, Shaoliang Li, Shaoliang
	Futaki, Sugiko Futaki, Sugiko
	Sekiguchi, Kiyotoshi Sekiguchi, Kiyotoshi
内容	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
抄録	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.
公開者	American Society for Biochemistry and Molecular Biology
掲載誌名	Journal of Biological Chemistry
巻	282
号	15
開始ページ	11144
終了ページ	11154
刊行年月	2007-04
ISSN	1083351X
NCID	AA1202441X
DOI	info:doi/10.1074/jbc.M609402200
URL	http://hdl.handle.net/11094/71428
言語	英語
カテゴリ	学術雑誌論文 Journal Article

著者版フラグ	publisher
NII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.282(15) P.11144-P.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	英語
DCTERMS.issued" scheme="DCTERMS.W3CDTF	2007-04
DC.identifier	info:doi/10.1074/jbc.M609402200
DC.identifier" scheme="DCTERMS.URI	http://hdl.handle.net/11094/71428
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.
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	英語
citation_date	2007-04
citation_journal_title	Journal of Biological Chemistry
citation_volume	282
citation_issue	15
citation_firstpage	11144
citation_lastpage	11154
citation_issn	1083351X
citation_doi	info:doi/10.1074/jbc.M609402200
citation_public_url	http://hdl.handle.net/11094/71428

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