Estrogen receptor activation function 1 works by binding p160 coactivator proteins

P. Webb, P. Nguyen, J. Shinsako, C. Anderson, W. Feng, M. P. Nguyen, D. Chen, S. M. Huang, S. Subramanian, E. McKinerney, B. S. Katzenellenbogen, M. R. Stallcup, P. J. Kushner

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341 Scopus citations


Estrogen receptor-α contains two transactivation functions, a weak constitutive activation function (AF-1) and a hormone-dependent activation function (AF-2). AF-2 works by recruiting a large coactivator complex, composed of one or more p160s, CREB-binding protein (CBP)/p300, and P/CAF (p300 and CBP-associated factor), via direct contacts with the p160s. We report here that independent AF-1 activity also requires p160 contacts. Unlike AF-2, which binds signature NR boxes in the center of the p160 molecule, AF-1 binds to sequences near the p160 C terminus. We propose that the ability of AF-1 and AF-2 to interact with separate surfaces of the same coactivator is important for the ability of these transactivation functions to synergize.

Original languageEnglish (US)
Pages (from-to)1605-1618
Number of pages14
JournalMolecular Endocrinology
Issue number10
StatePublished - 1998

ASJC Scopus subject areas

  • Molecular Biology
  • Endocrinology


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