Glycosylation of the murine estrogen receptor-alpha

J Steroid Biochem Mol Biol. 2000 Dec 15;75(2-3):147-58. doi: 10.1016/s0960-0760(00)00167-9.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetylglucosamine / chemistry*
  • Acetylglucosamine / metabolism
  • Amino Acid Sequence
  • Animals
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Estrogen Receptor alpha
  • Galactosyltransferases / metabolism
  • Glycosylation
  • Mice
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Mapping
  • Peptides / chemistry
  • Protein Processing, Post-Translational*
  • Receptors, Estrogen / chemistry*
  • Receptors, Estrogen / genetics
  • Receptors, Estrogen / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Transfection
  • Trypsin / metabolism


  • Estrogen Receptor alpha
  • Peptides
  • Receptors, Estrogen
  • Recombinant Proteins
  • Galactosyltransferases
  • Trypsin
  • Acetylglucosamine