期刊
FEBS LETTERS
卷 583, 期 19, 页码 3285-3290出版社
WILEY
DOI: 10.1016/j.febslet.2009.09.001
关键词
Adhesion-G protein-coupled receptor; Auto-proteolysis; G protein-coupled receptor proteolytic site; N-Glycosylation
资金
- National Science Council [NSC96-2320-B-182-005]
- Chang Gung Memorial Hospital [CMRPD170012]
- MRC [G0500623] Funding Source: UKRI
- Medical Research Council [G0500623] Funding Source: researchfish
Auto-proteolysis at the G protein-coupled receptor (GPCR) proteolytic site (GPS) is a hallmark of adhesion-GPCRs. Although defects in GPS auto-proteolysis have been linked to genetic disorders, information on its regulation remains elusive. Here, we investigated the GPS proteolysis of CD97, a human leukocyte-restricted and tumor-associated adhesion-GPCR. We found that CD97 is incompletely processed, unlike its close homolog, epidermal growth factor-like module-containing mucin-like hormone receptor 2. A unique pattern of N-glycosylation within the GPS motif of related adhesion-GPCRs was identified. The use of N-glycosylation inhibitors and mutants confirm site-specific N-glycosylation is an important determinant of GPS proteolysis in CD97. Our results suggest that N-glycosylation may regulate the processing of adhesion-GPCRs leading to the production of either cleaved or uncleaved molecules. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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