Author(s): Tanabe K, Nagata K, Ohashi K, Nakano T, Arita H,
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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 gamma-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 gamma-carboxylation of the Gla domain has a regulatory role in retaining the activity of native Gas6.
This article was published in FEBS Lett
and referenced in Journal of Addiction Research & Therapy