O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits.

Wells L, Kreppel LK, Comer FI, Wadzinski BE, Hart GW
J Biol Chem. 2004 279 (37): 38466-70

PMID: 15247246 · DOI:10.1074/jbc.M406481200

A hallmark of signal transduction is the dynamic and inducible post-translational modification of proteins. In addition to the well characterized phosphorylation of proteins, other modifications have been shown to be regulatory, including O-linked beta-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modifies serine and threonine residues on a myriad of nuclear and cytosolic proteins, and for several proteins there appears to be a reciprocal relationship between phosphorylation and O-GlcNAc modification. Here we report further evidence of this yin-yang relationship by demonstrating that O-GlcNAc transferase, the enzyme that adds O-GlcNAc to proteins, exists in stable and active complexes with the serine/threonine phosphatases PP1beta and PP1gamma, enzymes that remove phosphate from proteins. The existence of this complex highlights the importance of understanding the dynamic relationship between O-GlcNAc and phosphate in modulating protein function in many cellular processes and disease states such as Alzheimer's disease and type II diabetes.

MeSH Terms (23)

Animals Blotting, Western Brain Catalytic Domain Cell Nucleus Chromatography Chromatography, Gel Chromatography, Liquid Cytosol Mass Spectrometry N-Acetylglucosaminyltransferases Phosphoprotein Phosphatases Phosphoric Monoester Hydrolases Phosphorylation Precipitin Tests Protein Binding Protein Isoforms Protein Phosphatase 1 Protein Structure, Tertiary Rats Serine Signal Transduction Threonine

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