O-GlcNAc transferase is in a functional complex with protein phosphatase 1 catalytic subunits - PubMed (original) (raw)

. 2004 Sep 10;279(37):38466-70.

doi: 10.1074/jbc.M406481200. Epub 2004 Jul 7.

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

Lance Wells et al. J Biol Chem. 2004.

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Abstract

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.

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