Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*
Arshad N, Ballal S, Visweswariah SS. Site-specific N-Linked Glycosylation of Receptor Guanylyl Cyclase C Regulates Ligand Binding, Ligand-mediated Activation and Interaction with Vesicular Integral Membrane Protein 36, VIP36*. Journal Of Biological Chemistry 2012, 288: 3907-3917. PMID: 23269669, PMCID: PMC3567644, DOI: 10.1074/jbc.m112.413906.Peer-Reviewed Original ResearchMeSH KeywordsCell LineCell MembraneEndoplasmic ReticulumGastrointestinal HormonesGlycosylationHumansLigandsMannose-Binding LectinsMembrane Transport ProteinsNatriuretic PeptidesProtein BindingProtein FoldingProtein Structure, TertiaryReceptors, EnterotoxinReceptors, Guanylate Cyclase-CoupledReceptors, PeptideConceptsLigand bindingVesicular integral membrane proteinGuanylyl cyclase CIntegral membrane proteinsGlycosylation of proteinsHeat‐stable enterotoxin peptideLigand-mediated activationSite of glycosylationTissue-dependent mannerReceptor guanylyl cyclaseReceptor guanylyl cyclase CGlycan-mediated interactionsDifferent cell typesMembrane proteinsSystematic mutagenesisGlycosylation sitesCyclase CCGMP-dependent mannerExtracellular domainProtein 36Endoplasmic reticulumSurface localizationVIP36Cell typesST peptides