Roles of γ‐carboxylation and a sex hormone‐binding globulin‐like domain in receptor‐binding and in biological activities of Gas6
Open Access
- 26 May 1997
- journal article
- Published by Wiley in FEBS Letters
- Vol. 408 (3) , 306-310
- https://doi.org/10.1016/s0014-5793(97)00448-1
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.Keywords
This publication has 23 references indexed in Scilit:
- Identification of the Product of Growth Arrest-specific Gene 6 as a Common Ligand for Axl, Sky, and Mer Receptor Tyrosine KinasesJournal of Biological Chemistry, 1996
- Prevention of growth arrest‐induced cell death of vascular smooth muscle cells by a product of growth arrest‐specific gene, gas6FEBS Letters, 1996
- Characterization of a high‐affinity and specific binding site for Gas6FEBS Letters, 1996
- Characterization of Gas6, a Member of the Superfamily of G Domain-containing Proteins, as a Ligand for Rse and AxlJournal of Biological Chemistry, 1996
- Stimulation of Sky Receptor Tyrosine Kinase by the Product of Growth Arrest-specific Gene 6Journal of Biological Chemistry, 1995
- Reevaluation of the roles of protein S and gas6 as ligands for the receptor tyrosine kinase Rse/Tyro 3Cell, 1995
- Vascular Smooth Muscle Cell-derived, Gla-containing Growth-potentiating Factor for Ca2+-mobilizing Growth FactorsJournal of Biological Chemistry, 1995
- Axl receptor tyrosine kinase stimulated by the vitamin K-dependent protein encoded by growth-arrest-specific gene 6Nature, 1995
- The molecular basis of blood coagulationCell, 1988
- Interactions of Protein S with MembranesSeminars in Thrombosis and Hemostasis, 1988