Distinct Roles of N-Glycosylation at Different Sites of Corin in Cell Membrane Targeting and Ectodomain Shedding

• DOI: 10.1074/jbc.m114.606442
• Publication Date: 2014-12-02T07:37:36Z
• Authors: Hao Wang; Tiantian Zhou; Jianhao Peng; Ping Xu; Ningzheng Dong; Shenghan Chen; Qingyu Wu
• Keywords: Ectodomain; N-linked glycosylation; Zymogen; Cell membrane; Tunicamycin

Corin is a membrane-bound protease essential for activating natriuretic peptides and regulating blood pressure. Human corin has 19 predicted N-glycosylation sites in its extracellular domains. It been shown that N-glycans are required cell surface expression zymogen activation. remains unknown, however, how at different may regulate biosynthesis processing. In this study, we examined mutants, which each of the was mutated individually. By Western analysis proteins lysate conditioned medium from transfected HEK293 cells HL-1 cardiomyocytes, found Asn-80 inhibited shedding juxtamembrane domain. Similarly, Asn-231 protected autocleavage frizzled-1 Moreover, Asn-697 scavenger receptor domain Asn-1022 important targeting We also location site not critical. N-Glycosylation be switched to promote Together, our results show play distinct roles membrane targeting, activation, ectodomain corin.Corin transmembrane containing sites.ResultsCorin mutants lacking individual were studied their processing.ConclusionN-Glycosylation plays preventing promoting activation.SignificanceThe understanding activity regulated. sites.