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- Title
Dynamic Cycling of the O-GlcNAc Transferase on the Estrogen Responsive pS2 Promoter During the Transcription Cycle.
- Authors
Sakabe, Kaoru; Hart, Gerald W.
- Abstract
Enzymatic modification of serine and threonine residues on nucleocytoplasmic proteins with a single N-acetylglucosamine moiety through a ?-glycosidic linkage (O-GlcNAc) is a dynamic posttranslational modification. Much like phosphorylation, protein O-GlcNAcylation is responsive to cell stimuli and can serve to regulate protein function. However, while there are a large number of different kinases and phosphatases, only a single O-GlcNAc Transferase (OGT) and O-GlcNAcase have been identified in mammals. Recently, through a yeast two-hybrid approach, we have identified Coactivator Associated Arginine Methyltransferase (CARM1) as a putative binding partner with OGT. CARM1 has been shown by other groups to methylate Arg residues of proteins such as p300 and histone H3. Additionally, CARM1 is required for maximal transcriptional activation of nuclear hormone receptor mediated transcription. Furthermore, CARM1, as well as other components of the transcriptional machinery, associates cyclically with the estrogen responsive pS2 promoter. We have recently shown that not only does CARMI bind OGT, but also it itself is an O-GlcNAc modified protein. Our data indicate that the O-GlcNAc processing enzymes also cycle on and off the pS2 promoter and are involved in the transcription regulation at the pS2 promoter.
- Subjects
GLYCOSIDES; ESTROGEN; PROTEINS; METHYLTRANSFERASES; ENZYMES
- Publication
FASEB Journal, 2007, Vol 21, Issue 5, pA286
- ISSN
0892-6638
- Publication type
Article
- DOI
10.1096/fasebj.21.5.a286