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Background  N-acetylglucosaminyltransferase-III (GnT-III) is a glycosyltransferase encoded by  Mgat3  that catalyzes the addition of β1,4-bisecting-N-acetylglucosamine on N-glycans. GnT-III has been pointed as a metastases suppressor having varying effects on cell adhesion and migration. We have previously described the existence of a functional feedback loop between E-cadherin expression and GnT-III-mediated glycosylation. The effects of GnT-III-mediated glycosylation on E-cadherin expression and cellular phenotype lead us to evaluate  Mgat3  and GnT-III-glycosylation role during Epithelial-Mesenchymal-Transition (EMT) and the reverted process, Mesenchymal-Epithelial-Transition (MET).    Methodology/Principal Findings  We analyzed the expression profile and genetic mechanism controlling  Mgat3  expression as well as GnT-III-mediated glycosylation, in general and specifically on E-cadherin, during EMT/MET. We found that during EMT,  Mgat3  expression was dramatically decreased and later recovered when cells returned to an epithelial-like phenotype. We further identified that  Mgat3  promoter methylation/demethylation is involved in this expression regulation. The impact of  Mgat3  expression variation, along EMT/MET, leads to a variation in the expression levels of the enzymatic product of GnT-III (bisecting GlcNAc structures), and more importantly, to the specific modification of E-cadherin glycosylation with bisecting GlcNAc structures.    Conclusions/Significance  Altogether, this work identifies for the first time  Mgat3  glycogene expression and GnT-III-mediated glycosylation, specifically on E-cadherin, as a novel and major component of the EMT/MET mechanism signature, supporting its role during EMT/MET.

Loss and Recovery of Mgat3 and GnT-III Mediated E-cadherin N-glycosylation Is a Mechanism Involved in Epithelial-Mesenchymal-Epithelial Transitions