Glycosylation of the murine estrogen receptor-α

X. Cheng, Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)147-158
Number of pages12
JournalJournal of Steroid Biochemistry and Molecular Biology
Volume75
Issue number2-3
DOIs
StatePublished - Dec 15 2000

Keywords

  • Estrogen
  • Estrogen receptor
  • O-GlcNAc
  • O-glycosylation
  • PEST domain
  • Phosphorylation
  • Post-translational modification

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

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