Abstract
O-linked N-acetylglucosamine (O-GlcNAc) is a highly dynamic and abundant modification found on nuclear and cytoplasmic proteins of nearly all eukaryotes. O-GlcNAc addition is required for life at the single cell level and is analogous to protein phosphorylation in most respects. In a previous study (M.S. Jiang, G.W. Hart, A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine. J. Biol. Chem. 270 (1997) 2421-2428), we demonstrated that a subpopulation of the murine estrogen receptor-α (mER-α) is modified by O-GlcNAc at Thr575. Here we mutated mER-α to convert Thr575 and Ser576 to Val and Ala, respectively. Surprisingly, this glycosylation-site mutant is still extensively modified by O-GlcNAc. Analyses of glycopeptides identified two additional sites of modification on mER-α, at Ser10 and Thr50 near the N-terminus. The major glycosylation sites are within or near PEST regions, suggesting that O-GlcNAc may regulate mER-α turnover.
Original language | English (US) |
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Pages (from-to) | 147-158 |
Number of pages | 12 |
Journal | Journal of Steroid Biochemistry and Molecular Biology |
Volume | 75 |
Issue number | 2-3 |
DOIs | |
State | Published - Dec 15 2000 |
Keywords
- Estrogen
- Estrogen receptor
- O-GlcNAc
- O-glycosylation
- PEST domain
- Phosphorylation
- Post-translational modification
ASJC Scopus subject areas
- Biochemistry
- Endocrinology