O-Linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell–matrix interactions

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O-linked-N-acetylglucosamine on extracellular protein domains mediates epithelial cell-matrix interactions.

The O-linked-N-acetylglucosamine (O-GlcNAc) modification of cytoplasmic and nuclear proteins regulates basic cellular functions and is involved in the aetiology of diabetes and neurodegeneration. This intracellular O-GlcNAcylation is catalyzed by a single O-GlcNAc transferase, OGT. Here we report a novel OGT, EOGT, responsible for extracellular O-GlcNAcylation. Although both OGT and EOGT are re...

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The addition of O-linked N-acetylglucosamine (O-GlcNAc) to target proteins may serve as a signaling modification analogous to protein phosphorylation. Like phosphorylation, O-GlcNAc is a dynamic modification occurring in the nucleus and cytoplasm. Various analytical methods have been developed to detect O-GlcNAc and distinguish it from glycosylation in the endomembrane system. Many target molec...

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Discovering Domains Mediating Protein Interactions

Background: Protein-protein interactions do not provide any direct information re‌garding the domains within the proteins that mediate the interactions. The majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. Most of the former studies focus only on interacting do‌main pairs. However they do not consider the in...

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ژورنال

عنوان ژورنال: Nature Communications

سال: 2011

ISSN: 2041-1723

DOI: 10.1038/ncomms1591