Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions.

Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Research Abstract Details 

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Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Abstract Text:

Akiko Koide,Changqing Zhao,Misuzu Naganuma,Judith Abrams,Sarah Deighton-Collins,Debra F Skafar,Shohei Koide,

The estrogen receptor (ER)alpha is a biologically and clinically important ligand-modulated transcription factor. The F domain of the ERalpha modulates its functions in a ligand-, promoter-, and cell-specific manner. To identify the region(s) responsible for these functions, we characterized the effects of serial truncations within the F domain. We found that truncating the last 16 residues of the F domain altered the activity of the human ERalpha (hERalpha) on an estrogen response element-driven promoter in response to estradiol or 4-hydroxytamoxifen (4-OHT), its sensitivity to overexpression of the coactivator steroid receptor coactivator-1 in mammalian cells, and its interaction with a receptor-interacting domain of the coactivator steroid receptor coactivator-1 or engineered proteins ("monobodies") that specifically bind to ERalpha/ligand complexes in a yeast two-hybrid system. Most importantly, the ability of the ER to induce pS2 was reduced in MDA-MB-231 cells stably expressing this truncated ER vs. the wild-type ER. The region includes a distinctive segment (residues 579-584; LQKYYIT) having a high content of bulky and/or hydrophobic amino acids that was previously predicted to adopt a beta-strand-like structure. As previously reported, removal of the entire F domain was necessary to eliminate the agonist activity of 4-OHT. In addition, mutation of the vicinal glycine residues between the ligand-binding domain and F domains specifically reduced the 4-OHT-dependent interactions of the hERalpha ligand-binding domain and F domains with monobodies. These results show that regions within the F domain of the hERalpha selectively modulate its activity and its interactions with other proteins.

Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Publishing Authors By Initials

A Koide,C Zhao,M Naganuma,J Abrams,S Deighton-Collins,DF Skafar,S Koide,

For similar proteins: transcription factors research abstracts see: proteins: transcription factors research

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Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Molecular endocrinology (Baltimore, Md.)

VOLUME: 21

Page Numbers: 829-42

Journal Abbreviation: Mol. Endocrinol.

ISSN: 0888-8809

DAY: 21

MONTH: 12

YEAR: 2006

Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8801431

Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Keywords Mesh Terms:

KEYWORDS: Transcription Factors

MESH TERMS: genetics

Chemical & Substance for Abstract: Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions. Information

Substance Name: nuclear receptor coactivator 1

Registry Number: EC 2.3.1.48

Grant and Affiliation Information for Identification of regions within the F domain of the human estrogen receptor alpha that are important for modulating transactivation and protein-protein interactions.

AFFILIATION: Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, Illinois 60637, USA.

Country: United States

AGENCY: United States NIDDK

GRANT: R01 DK63090

ACRONYM: DK

MEDLINETA: Mol Endocrinol

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