In mice, but not in humans, the bone-derived hormone osteocalcin is O-glycosylated, a post-translational modification controlling its half-life in vivo.
The first inhibitor identified against an iso-enzyme that initiates O-glycosylation in the Golgi complex promises new therapeutic approaches for cancer and chronic kidney disease.
T antigen glycosylation, which marks metastatic cancer cells, is modulated on a small set of proteins by a conserved multipass transmembrane protein to allow tissue invasion by Drosophila macrophages.
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 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.
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.
A protein modification called O-linked glycosylation regulates the interactions between vimentin molecules under normal conditions, and the ability of Chlamydia bacteria to replicate after they infect cells.
A single mutation in Escherichia coli connects two essential cell envelope assembly pathways and confers vancomycin resistance by displaying molecular decoys at the cell surface.
Glycosylation of flagellins with pseudaminic acid in the bacterial cytoplasm governed by an unknown type of modular glycosyltransferase harboring an N-terminal substrate binding domain and a C-terminal glycosyltransferase domain.
