Roles of γ-carboxylation and a sex hormone-binding globulin-like domain in receptor-binding and in biological activities of Gas6

Kazuyo Tanabe, Kyoko Nagata, Kazumasa Ohashi, Toru Nakano, Hitoshi Arita, Kensaku Mizuno

研究成果: Article査読

42 被引用数 (Scopus)

抄録

Gas6 is a ligand for an Axl/Sky receptor tyrosine kinase subfamily and has a structure composed of a Gla domain, four EGF-like domains and a C-terminal sex hormone-binding globulin (SHBG)-like domain. When examining the role of each domain in receptor-binding and biological activities of Gas6, we found that receptor-binding and mitogenic activities were markedly reduced by inhibiting γ-carboxylation of the Gla domain, while a Gas6 mutant composed of only an SHBG-like domain retained both of these activities. Thus, the SHBG-like domain is apparently an entity indispensable for Gas6 activities, and γ-carboxylation of the Gla domain has a regulatory role in retaining the activity of native Gas6.

本文言語English
ページ(範囲)306-310
ページ数5
ジャーナルFEBS Letters
408
3
DOI
出版ステータスPublished - 1997 5 26

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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