6 results found
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics

    Structure of protein O-mannose kinase reveals a unique active site architecture

    Qinyu Zhu et al.
    Active site migration establishes kinase activity in protein O-mannose kinase.
    1. Biochemistry and Chemical Biology

    POMK regulates dystroglycan function via LARGE1-mediated elongation of matriglycan

    Ameya S Walimbe et al.
    Protein O-Mannose Kinase enables Like-acetyl-glucosaminyltransferase 1 to elongate matriglycan on α-dystroglycan, thereby allowing matriglycan to function as a scaffold for extracellular matrix proteins and prevent muscular dystrophy.
    1. Biochemistry and Chemical Biology

    B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan

    Jeremy L Praissman et al.
    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.
    1. Cell Biology
    2. Neuroscience

    High N-glycan multiplicity is critical for neuronal adhesion and sensitizes the developing cerebellum to N-glycosylation defect

    Daniel Medina-Cano et al.
    Impairment of protein N-glycosylation disrupts neural cell adhesion mediated by highly glycosylated members of the IgSF-CAM protein family.
    1. Biochemistry and Chemical Biology

    The glucuronyltransferase B4GAT1 is required for initiation of LARGE-mediated α-dystroglycan functional glycosylation

    Tobias Willer et al.
    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.
    1. Biochemistry and Chemical Biology

    The functional O-mannose glycan on α-dystroglycan contains a phospho-ribitol primed for matriglycan addition

    Jeremy L Praissman et al.
    Disruption of the LG domain-binding phospho-ribitol-containing O-mannose structures on α-dystroglycan results in congenital muscular dystrophy.

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