Interaction of proteins with transcriptionally active estrogen receptors
- PMID: 7937828
- PMCID: PMC44947
- DOI: 10.1073/pnas.91.21.10009
Interaction of proteins with transcriptionally active estrogen receptors
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.
Similar articles
-
The quinone reductase gene: a unique estrogen receptor-regulated gene that is activated by antiestrogens.Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2581-6. doi: 10.1073/pnas.94.6.2581. Proc Natl Acad Sci U S A. 1997. PMID: 9122238 Free PMC article.
-
Human estrogen receptor ligand activity inversion mutants: receptors that interpret antiestrogens as estrogens and estrogens as antiestrogens and discriminate among different antiestrogens.Mol Endocrinol. 1996 Mar;10(3):230-42. doi: 10.1210/mend.10.3.8833652. Mol Endocrinol. 1996. PMID: 8833652
-
Specific mutations in the estrogen receptor change the properties of antiestrogens to full agonists.Proc Natl Acad Sci U S A. 1995 May 9;92(10):4206-10. doi: 10.1073/pnas.92.10.4206. Proc Natl Acad Sci U S A. 1995. PMID: 7753783 Free PMC article.
-
Responses to pure antiestrogens (ICI 164384, ICI 182780) in estrogen-sensitive and -resistant experimental and clinical breast cancer.Ann N Y Acad Sci. 1995 Jun 12;761:148-63. doi: 10.1111/j.1749-6632.1995.tb31376.x. Ann N Y Acad Sci. 1995. PMID: 7625718 Review. No abstract available.
-
Mechanisms of antihormone action.J Steroid Biochem Mol Biol. 1992 Mar;41(3-8):217-21. doi: 10.1016/0960-0760(92)90347-l. J Steroid Biochem Mol Biol. 1992. PMID: 1562505 Review.
Cited by
-
Nuclear receptors: from molecular mechanisms to therapeutics.Essays Biochem. 2021 Dec 17;65(6):847-856. doi: 10.1042/EBC20210020. Essays Biochem. 2021. PMID: 34825698 Free PMC article.
-
The Role of Histone Deacetylase 3 Complex in Nuclear Hormone Receptor Action.Int J Mol Sci. 2021 Aug 24;22(17):9138. doi: 10.3390/ijms22179138. Int J Mol Sci. 2021. PMID: 34502048 Free PMC article. Review.
-
Targeting the NCOA3-SP1-TERT axis for tumor growth in hepatocellular carcinoma.Cell Death Dis. 2020 Nov 25;11(11):1011. doi: 10.1038/s41419-020-03218-x. Cell Death Dis. 2020. PMID: 33239622 Free PMC article.
-
Recent advances in the epidemiology and genetics of acute intermittent porphyria.Intractable Rare Dis Res. 2020 Nov;9(4):196-204. doi: 10.5582/irdr.2020.03082. Intractable Rare Dis Res. 2020. PMID: 33139978 Free PMC article. Review.
-
Detection of nucleic acid-protein interactions in plant leaves using fluorescence lifetime imaging microscopy.Nat Protoc. 2017 Sep;12(9):1933-1950. doi: 10.1038/nprot.2017.076. Epub 2017 Aug 24. Nat Protoc. 2017. PMID: 28837131
References
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources