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Proteomic analysis of steady-state nuclear hormone receptor coactivator complexes.

We report our initial efforts in the analysis of endogenous nuclear receptor coactivator complexes as a research bridging strand of the Nuclear Receptor Signaling Atlas (NURSA) (www.NURSA.org). A proteomic approach is used to systematically isolate a variety of coactivator complexes using HeLa cells as a model cell line and to identify the coactivator-associated proteins with mass spectrometry. We have isolated and identified seven coactivator complexes including the p160 steroid receptor coactivator family, cAMP response element binding protein-binding protein, p300, coactivator of activating protein-1 and estrogen receptors, and E6 papillomavirus-associated protein. The newly identified coactivator-associated proteins provide unbiased clues and links for understanding of the endogenous hormone receptor coregulator network and its regulation. We hope that the electronic availability of these data to the general scientific community will facilitate generation and testing of new hypotheses to further our understanding of nuclear receptor signaling and coactivator functions.

Pubmed ID: 16051665

Authors

  • Jung SY
  • Malovannaya A
  • Wei J
  • O'Malley BW
  • Qin J

Journal

Molecular endocrinology (Baltimore, Md.)

Publication Data

October 27, 2005

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK62434
  • Agency: NICHD NIH HHS, Id: HD08818

Mesh Terms

  • Antibodies
  • Cross Reactions
  • Databases, Protein
  • HeLa Cells
  • Humans
  • Mass Spectrometry
  • Multiprotein Complexes
  • Proteomics
  • Receptors, Cytoplasmic and Nuclear
  • Signal Transduction
  • Trans-Activators