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PMID: 7937828 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Interaction of proteins with transcriptionally active estrogen receptors.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 21 ·1994-10-11 ·Pages 10009-13

Cavaillès V, Dauvois S, Danielian PS, Parker MG

Abstract

The ligand binding domain of the estrogen receptor contains a hormone-dependent transcriptional activation function. To investigate the mechanism by which it stimulates transcription, we have expressed fusion proteins containing either the wild-type or a transcriptionally defective form of this domain fused to glutathione-S-transferase and searched for proteins that specifically interact in vitro. By far-Western blotting, three proteins of 160, 140, and 80 kDa expressed in different mammalian cells (HeLa, ZR75-1, and COS-1) were shown to associate directly with the wild-type receptor in the presence of estrogen. Two additional proteins appeared to interact indirectly with the hormone binding domain since they were detected only by a pull-down assay. All of these interactions were abolished by antiestrogens, such as 4-hydroxytamoxifen, ICI 164384, or ICI 182780, which inhibit hormone-dependent transcription. Moreover, they were not observed with the transcriptionally defective form of the receptor even in the presence of estrogen. Thus, since the ability of these proteins to interact with the hormone binding domain correlates with its transcriptional activity, one or more of them may contribute to hormone-dependent transcriptional activation by the estrogen receptor.

MeSH Terms
Animals Base Sequence Blotting, Western Cell Line Cell Nucleus/metabolism Cell-Free System Chlorocebus aethiops DNA Primers DNA-Binding Proteins/biosynthesis,metabolism Estradiol/analogs & derivatives,pharmacology Estrogen Antagonists/pharmacology Fulvestrant Glutathione Transferase/biosynthesis HeLa Cells Humans Kidney Molecular Sequence Data Nuclear Proteins/isolation & purification,metabolism Polyunsaturated Alkamides Receptors, Estrogen/biosynthesis,metabolism Recombinant Fusion Proteins/biosynthesis,metabolism Tamoxifen/analogs & derivatives,pharmacology Transcription, Genetic/drug effects
Chemicals
DNA Primers DNA-Binding Proteins Estrogen Antagonists Nuclear Proteins Polyunsaturated Alkamides Receptors, Estrogen Recombinant Fusion Proteins Tamoxifen afimoxifene Fulvestrant Estradiol ICI 164384 Glutathione Transferase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Cavaillès V
Molecular Endocrinology Laboratory, Imperial Cancer Research Fund, London, United Kingdom.
Dauvois S
Danielian P S
Parker M G
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44 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.21.10009
Published
1994-10-11
Pages
10009-13
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC44947
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.91.21.10009 PMC Full Text View journal details
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