期刊
FEBS LETTERS
卷 582, 期 16, 页码 2387-2392出版社
WILEY
DOI: 10.1016/j.febslet.2008.05.042
关键词
unconventional protein secretion; non-classical export; protein targeting; fibroblast growth factor 2; glycosylation; glycosaminoglycans; heparan sulfate proteoglycans; chondroitin sulfate
FGF-2 is a proangiogenic growth factor secreted by unconventional means. It is unknown why FGF-2 takes an ER/Golgi- independent secretory route. We find that secretion of FGF-2 via the ER/Golgi system causes post-translational modi. cations that prevent binding to heparan sulfate proteoglycans (HSPGs), an interaction that is critically important for both FGF-2 storage and signal transduction. This loss of function is due to artificial O-glycosylation mainly resulting in the addition of glycosaminoglycan chains of the chrondroitin sulfate type. Our findings suggest that the unconventional mechanism of FGF-2 export is an ancient pathway of protein secretion that, in the course of evolution, has been kept due to the inability of the classical secretory pathway to export FGF-2 in a functional form. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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