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PMID:8999954
| Citation |
Jiang, MS and Hart, GW (1997) A subpopulation of estrogen receptors are modified by O-linked N-acetylglucosamine. J. Biol. Chem. 272:2421-8 |
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| Abstract |
Estrogen receptors (ER) are ligand-inducible transcription factors regulated by Ser(Thr)-O-phosphorylation. Many transcription factors and eukaryotic RNA polymerase II itself are also dynamically modified by Ser(Thr)-O-linked N-acetylglucosamine moieties (O-GlcNAc). Here we report that subpopulations of murine, bovine, and human estrogen receptors are modified by O-GlcNAc. O-GlcNAc moieties were detected on insect cell-expressed, mouse ER (mER) by probing with bovine milk galactosyltransferase, followed by structural analysis. Wheat germ agglutinin-Sepharose affinity chromatography also readily detected terminal GlcNAc residues on subpopulations of ER purified from calf uterus, from human breast cancer cells (MCF-7), or from mER produced by in vitro translation. These data suggest that greater than 10% of these populations of estrogen receptors bear O-GlcNAc. Site mapping of insect cell expressed mER localized one major site of O-GlcNAc addition to Thr-575, within a PEST region of the carboxyl-terminal F domain. Based upon their relative resistance to both hexosaminidase and to in vitro galactosylation, O-GlcNAc moieties appear to be largely buried on native mER. This dynamic saccharide modification, like phosphorylation, may play a role in modulating the dimerization, stability, or transactivation functions of estrogen receptors. |
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| Keywords |
Acetylglucosamine/metabolism; Amino Acid Sequence; Animals; Cattle; Chromatography, Affinity; Chromatography, Gel; Chromatography, High Pressure Liquid; Female; Galactose/metabolism; Humans; Mice; Molecular Sequence Data; Receptors, Estrogen/metabolism; Structure-Activity Relationship; Tumor Cells, Cultured |
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Significance
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| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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