Title : Glycosylation of the murine
estrogen receptor-alpha
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-alpha ( mER-alpha) is modified by O-GlcNAc at Thr(575)
- Here we mutated mER-alpha to convert Thr(575) and Ser(576) 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-alpha, at Ser(10) and Thr(50) near the N-terminus
- The major glycosylation sites are within or near PEST regions , suggesting that O-GlcNAc may regulate mER-alpha turnover