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 β-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/tlireonine phosphatases PP1β and PP1γ, 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.
Original language | English (US) |
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Pages (from-to) | 38466-38470 |
Number of pages | 5 |
Journal | Journal of Biological Chemistry |
Volume | 279 |
Issue number | 37 |
DOIs | |
State | Published - Sep 10 2004 |
ASJC Scopus subject areas
- Biochemistry