Journal
FEBS LETTERS
Volume 585, Issue 2, Pages 313-318Publisher
WILEY
DOI: 10.1016/j.febslet.2010.12.005
Keywords
CD97; Homotypic cell-cell aggregation; N-cadherin; Epidermal growth factor module-containing seven-transmembrane receptor; GPCR proteolysis site autoproteolysis; G protein-coupled receptor
Funding
- National Science Council [NSC98-2320-B-182-028-MY3]
- Chang Gung Memorial Hospital [CMRPD170013, CMRPD160383]
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Most adhesion-class G protein-coupled receptors (adhesion-GPCRs) undergo a novel self-catalytic cleavage at the GPCR proteolysis site (GPS) to form a hetero-dimeric complex containing the extracellular and seven-span transmembrane subunits. However, little is known about the role of GPS auto-proteolysis in the function of adhesion-GPCRs. Here we show that GPS cleavage is essential for the homotypic cell aggregation promoted by CD97 receptor, a leukocyte-restricted adhesion-GPCR often aberrantly expressed in carcinomas. We find that CD97 does not mediate cell aggregation directly. Instead, expression of the wild type - but not the GPS cleavage-deficient CD97 upregulates the expression of N-cadherin, leading to Ca++-dependent cell-cell aggregation. Our results provide a clear evidence for the role of GPS proteolytic modification in the cellular function of adhesion-GPCRs. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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