The ERK8 kinase blocks the export of glycosyl-tranferases from the Golgi to the endoplasmic reticulum, and thus subsequent O-glycosylation of proteins that otherwise enhance cell motility and tissue invasion.
The correct enzymatic activity of a previously misnamed enzyme is defined, placing the enzyme upstream of LARGE in building functional O-mannose structures on α-dystroglycan that are disrupted in multiple forms of congenital muscular dystrophy.
Post-phosphoryl modification of α-dystroglycan requires the glucuronyltransferase B4GAT1; this enzyme synthesizes the acceptor glycan that serves as a primer for the glycosyltransferase LARGE to synthesize the laminin-binding glycan.
The cytoplasmic enzyme N-glycanase 1 plays an evolutionary conserved role in promoting the ERAD-mediated retrotranslocation of misfolded Dpp/BMP4 from the ER, thereby allowing BMP signaling in specific contexts.
The in vivo modification of the canonical intermediate filament protein vimentin with O-linked beta-N-acetylglucosamine affects its function in filament assembly, cell migration and host-pathogen interactions.