学術雑誌論文

学術雑誌論文

text

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

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

American Society for Biochemistry and Molecular Biology

英語

text

2007-04

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

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

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.

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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

American Society for Biochemistry and Molecular Biology

英語

2007-04

Journal of Biological Chemistry

282

15

11144

11154

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

https://hdl.handle.net/11094/71428