Calmodulin Enhances the Stability of the Estrogen Receptor *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 276, Issue: 20, Page: 17354-17360
2001
- 53Citations
- 12Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations53
- Citation Indexes53
- 53
- CrossRef45
- Captures12
- Readers12
- 12
Article Description
The estrogen receptor mediates breast cell proliferation and is the principal target for chemotherapy of breast carcinoma. Previous studies have demonstrated that the estrogen receptor binds to calmodulin-Sepharose in vitro. However, the association of endogenous calmodulin with endogenous estrogen receptors in intact cells has not been reported, and the function of the interaction is obscure. Here we demonstrate by co-immunoprecipitation from MCF-7 human breast epithelial cells that endogenous estrogen receptors bind to endogenous calmodulin. Estradiol treatment of the cells had no significant effect on the interaction. However, incubation of the cells with tamoxifen enhanced by 5–10-fold the association of calmodulin with the estrogen receptor and increased the total cellular content of estrogen receptors by 1.5–2-fold. In contrast, the structurally distinct calmodulin antagonists trifluoperazine and CGS9343B attenuated the interaction between calmodulin and the estrogen receptor and dramatically reduced the number of estrogen receptors in the cell. Neither of these agents altered the amount of estrogen receptor mRNA, suggesting that calmodulin stabilizes the protein. This hypothesis is supported by the observation that, in the presence of Ca 2+, calmodulin protected estrogen receptors from in vitro proteolysis by trypsin. Furthermore, overexpression of wild type calmodulin, but not a mutant calmodulin incapable of binding Ca 2+, increased the concentration of estrogen receptors in MCF-7 cells, whereas transient expression of a calmodulin inhibitor peptide reduced the estrogen receptor concentration. These data demonstrate that calmodulin binds to the estrogen receptor in intact cells in a Ca 2+ -dependent, but estradiol-independent, manner, thereby modulating the stability and the steady state level of estrogen receptors.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819319210; http://dx.doi.org/10.1074/jbc.m010238200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0035907380&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11278648; http://www.jbc.org/lookup/doi/10.1074/jbc.M010238200; https://syndication.highwire.org/content/doi/10.1074/jbc.M010238200; https://linkinghub.elsevier.com/retrieve/pii/S0021925819319210; https://dx.doi.org/10.1074/jbc.m010238200
American Society for Biochemistry & Molecular Biology (ASBMB)
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