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

doi:10.1210/mend.12.10.0185

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

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English (US)
Pages (from-to)	1605-1618
Number of pages	14
Journal	Molecular Endocrinology
Volume	12
Issue number	10
DOIs	https://doi.org/10.1210/mend.12.10.0185
State	Published - 1998
Externally published	Yes

ASJC Scopus subject areas

Molecular Biology
Endocrinology

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10.1210/mend.12.10.0185

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title = "Estrogen receptor activation function 1 works by binding p160 coactivator proteins",

abstract = "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.",

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

year = "1998",

doi = "10.1210/mend.12.10.0185",

language = "English (US)",

volume = "12",

pages = "1605--1618",

journal = "Molecular Endocrinology",

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publisher = "The Endocrine Society",

number = "10",

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TY - JOUR

T1 - Estrogen receptor activation function 1 works by binding p160 coactivator proteins

AU - Webb, P.

AU - Nguyen, P.

AU - Shinsako, J.

AU - Anderson, C.

AU - Feng, W.

AU - Nguyen, M. P.

AU - Chen, D.

AU - Huang, S. M.

AU - Subramanian, S.

AU - McKinerney, E.

AU - Katzenellenbogen, B. S.

AU - Stallcup, M. R.

AU - Kushner, P. J.

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

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JO - Molecular Endocrinology

JF - Molecular Endocrinology

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Estrogen receptor activation function 1 works by binding p160 coactivator proteins

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