Estrogen Receptor Activation Function 1 Works by Binding p160 Coactivator Proteins | Zendy

Paul Webb | Zendy; Phuong Nguyen | Zendy; J. Shinsako | Zendy; Carol M. Anderson | Zendy; Weijun Feng | Zendy; Mimi P. Nguyen | Zendy; Dagang Chen | Zendy; Shih-Ming Huang | Zendy; Sujatha Subramanian | Zendy; Eileen McKinerney | Zendy; Benita S. Katzenellenbogen | Zendy; Michael R. Stallcup | Zendy; Peter J. Kushner | Zendy

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Estrogen Receptor Activation Function 1 Works by Binding p160 Coactivator Proteins

Author(s) -

Paul Webb,

Phuong Nguyen,

J. Shinsako,

Carol M. Anderson,

Weijun Feng,

Mimi P. Nguyen,

Dagang Chen,

Shih-Ming Huang,

Sujatha Subramanian,

Eileen McKinerney,

Benita S. Katzenellenbogen,

Michael R. Stallcup,

Peter J. Kushner

Publication year - 1998

Publication title -

molecular endocrinology

Language(s) - English

Resource type - Journals

eISSN - 1944-9917

pISSN - 0888-8809

DOI - 10.1210/mend.12.10.0185

Subject(s) - transactivation , coactivator , nuclear receptor coactivator 3 , biology , creb binding protein , microbiology and biotechnology , nuclear receptor coactivator 2 , function (biology) , cancer research , transcription factor , creb , gene , genetics

Estrogen receptor-alpha 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.

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