title: Modulation of E-cadherin function and dysfunction by N-glycosylation.
abstract: Several mechanisms have been proposed to explain the E-cadherin dysfunction in cancer, including genetic and epigenetic alterations. Nevertheless, a significant number of human carcinomas have been seen that show E-cadherin dysfunction that cannot be explained at the genetic/epigenetic level. A substantial body of evidence has appeared recently that supports the view that other mechanisms operating at the post-translational level may also affect E-cadherin function. The present review addresses molecular aspects related to E-cadherin N-glycosylation and evidence is presented showing that the modification of N-linked glycans on E-cadherin can affect the adhesive function of this adhesion molecule. The role of glycosyltransferases involved in the remodeling of N-glycans on E-cadherin, including N-acetylglucosaminyltransferase III (GnT-III), N-acetylglucosaminyltransferase V (GnT-V), and the α1,6 fucosyltransferase (FUT8) enzyme, is also discussed. Finally, this review discusses an alternative functional regulatory mechanism for E-cadherin operating at the post-translational level, N-glycosylation, that may underlie the E-cadherin dysfunction in some carcinomas.
authors.affiliation: Institute of Molecular Pathology and Immunology University of Porto, Portugal.
authors.forename: Salomé S
authors.initials: SS
authors.lastname: Pinho
authors.forename: Raquel
authors.initials: R
authors.lastname: Seruca
authors.forename: Fátima
authors.initials: F
authors.lastname: Gärtner
authors.forename: Yoshiki
authors.initials: Y
authors.lastname: Yamaguchi
authors.forename: Jianguo
authors.initials: J
authors.lastname: Gu
authors.forename: Naoyuki
authors.initials: N
authors.lastname: Taniguchi
authors.forename: Celso A
authors.initials: CA
authors.lastname: Reis
mesh_terms: D015820:Cadherins / Q000378:metabolism*; D002277:Carcinoma / Q000378:metabolism* / Q000473:pathology; D002448:Cell Adhesion / Q000502:physiology; D006031:Glycosylation; D016695:Glycosyltransferases / Q000378:metabolism; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D011134:Polysaccharides / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D015820:Cadherins; D011134:Polysaccharides; D016695:Glycosyltransferases