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

Research output: Contribution to journalArticlepeer-review

41 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)306-310
Number of pages5
JournalFEBS Letters
Volume408
Issue number3
DOIs
Publication statusPublished - 1997 May 26

Keywords

  • Gas6
  • Gla domain
  • Sex hormone-binding globulin
  • γ-Carboxylation

ASJC Scopus subject areas

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

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