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Roles of γ‐carboxylation and a sex hormone‐binding globulin‐like domain in receptor‐binding and in biological activities of Gas6
Author(s) -
Tanabe Kazuyo,
Nagata Kyoko,
Ohashi Kazumasa,
Nakano Toru,
Arita Hitoshi,
Mizuno Kensaku
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00448-1
Subject(s) - gas6 , binding domain , receptor , biology , biochemistry , chemistry , receptor tyrosine kinase , binding site
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.