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J. Biol. Chem., Vol. 279, Issue 37, 38466-38470, September 10, 2004

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O-GlcNAc Transferase Is in a Functional Complex with Protein Phosphatase 1 Catalytic Subunits^*

Lance Wells, Lisa K. Kreppel, Frank I. Comer, Brian E. Wadzinski¶, and Gerald W. Hart||

From the Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205 and the ^¶Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

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 -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 PP1 and PP1, 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.

Received for publication, June 10, 2004 , and in revised form, July 7, 2004.

^* This work was supported in part by National Institutes of Health Grant HD13563 (to G. W. H.) and Grants GM51366 and GM62265 (to B. E. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602. E-mail: lwells{at}ccrc.uga.edu.

^|| To whom correspondence should be addressed. E-mail: gwhart{at}jhmi.edu.

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