期刊
JOURNAL OF CELLULAR BIOCHEMISTRY
卷 114, 期 4, 页码 816-822出版社
WILEY-BLACKWELL
DOI: 10.1002/jcb.24420
关键词
c-Met; GLYCOSYLATION; PHOSPHORYLATION; pro-Met
资金
- National Natural Science Foundation of China [81000886, 81170377]
- New Century Excellent Talents in University [NCET-11-1058]
c-Met, the receptor for hepatocyte growth factor (HGF), is cell surface tyrosine kinase that controls cancer cell growth, survival, invasion, and metastasis. Post-translational modification, such as glycosylation, plays an essential role in regulating the function of cell surface molecules. Whether glycosylation modification regulates the enzymatic properties of c-Met is unknown. In this study, we investigated the effect of glycosylation on the function of c-Met. We found that c-Met is an N-linked glycosylated protein. Both pro-Met and p145Met (the subunit of mature c-Met) have N-linked glycosylation. Glycosylation inhibitor studies revealed that the N-glycosylation modification of p145Met is from pro-Met, but not due to the further modification of pro-Met. Importantly, blocking the N-glycosylation targets pro-Met to cytoplasm and initiates its phosphorylation independent of HGF engagement. Nonglycosylated pro-Met activates c-Met downstream pathways to a certain extent to compensate for the degradation of p145Met induced by glycosylation blocking-mediated endoplasmic reticulum (ER) stress. J. Cell. Biochem. 114: 816822, 2013. (c) 2012 Wiley Periodicals, Inc.
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