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Article

Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability.

The Journal of biological chemistry - 28 Jul 2017

Willems Anke P, Gundogdu Mehmet, Kempers Marlies J E, Giltay Jacques C, Pfundt Rolph, Elferink Martin, Loza Bettina F, Fuijkschot Joris, Ferenbach Andrew T, van Gassen Koen L I, van Aalten Daan M F, Lefeber Dirk J

Abstract excerpt

N-Acetylglucosamine (O-GlcNAc) transferase (OGT) regulates protein O-GlcNAcylation, an essential and dynamic post-translational modification. The O-GlcNAc modification is present on numerous nuclear and cytosolic proteins and has been implicated in essential cellular functions such as signaling and gene expression. Accordingly, altered levels of protein O-GlcNAcylation have been associated with developmental...

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Identifiers

PMID: 28584052
DOI: 10.1074/jbc.M117.790097
PMCID: PMC5535036

Genes

OGT

Variants

Provenance

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Related research

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Research trail→

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Mutations in N-acetylglucosamine (O-GlcNAc) transferase in patients with X-linked intellectual disability.PMID 28584052Read ↗

Generation of an Unbiased Interactome for the Tetratricopeptide Repeat Domain of O-GlcNAc Transferase Indicates a Role for the Enzyme in Intellectual DisabilitySemantic proximity Read ↗

Systematic mapping of O-GlcNAc transferase and O-GlcNAcase defines disease-associated variants.Semantic proximity Read ↗

O-GlcNAc: Regulator of Signaling and Epigenetics Linked to X-linked Intellectual DisabilitySemantic proximity Read ↗

Intellectual disability and neurogenesis defects associated with increased turnover of an O-GlcNAcase variantSemantic proximity Read ↗

An O-GlcNAc transferase pathogenic variant that affects pluripotent stem cell self-renewalSemantic proximity Read ↗

Neurodevelopmental defects in a mouse model of O-GlcNAc transferase intellectual disability.Semantic proximity Read ↗

OGT ( <i>O</i> -GlcNAc Transferase) selectively modifies multiple residues unique to lamin ASemantic proximity Read ↗

Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT.Semantic proximity Read ↗

Ogt-dependent X-chromosome-linked protein glycosylation is a requisite modification in somatic cell function and embryo viability.Semantic proximity Read ↗

CRISPR-Cas9-mediated depletion of <i>O</i> -GlcNAc hydrolase and transferase for functional dissection of <i>O</i> -GlcNAcylation in human cellsSemantic proximity Read ↗

Mutational analysis of the catalytic domain of O-linked N-acetylglucosaminyl transferase.Semantic proximity Read ↗

Structural and Functional Characterization of N-Glycanase-1 Pathogenic VariantsSemantic proximity Read ↗

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