ArticleThe Journal of biological chemistry2012
Structural basis for Ca2+-induced activation and dimerization of estrogen receptor α by calmodulin.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Novel FRET-Based Biosensors for Real-Time Monitoring of Estrogen Receptor Dimerization and Translocation Dynamics in Living Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Chemical shift assignments of calmodulin under standard conditions at neutral pH.Biomolecular NMR assignments · 2022Article
- Calcium and calcium-related proteins in endometrial cancer: opportunities for pharmacological intervention.International journal of biological sciences · 2022Review
- Chemical shift assignments of the N-terminal domain of PSD95 (PSD95-NT).Biomolecular NMR assignments · 2021Article
- The Crystal Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues Phe4246-Val4271 Reveals a Fifth Calcium Binding Site.Biochemistry · 2021Article
- Dynamic NaeLife · 2021Article
- Computer-Aided Ligand Discovery for Estrogen Receptor Alpha.International journal of molecular sciences · 2020Review
- A Non-Canonical Calmodulin Target Motif Comprising a Polybasic Region and Lipidated Terminal Residue Regulates Localization.International journal of molecular sciences · 2020Review
- α-Actinin-1 promotes activity of the L-type CaThe EMBO journal · 2020Article
- Reciprocality Between Estrogen Biology and Calcium Signaling in the Cardiovascular System.Frontiers in endocrinology · 2020Review
- Estrogen Receptor β2 Oversees Germ Cell Maintenance and Gonadal Sex Differentiation in Medaka, Oryzias latipes.Stem cell reports · 2019Article
- Role of Resultant Dipole Moment in Mechanical Dissociation of Biological Complexes.Molecules (Basel, Switzerland) · 2018Article
- CaThe EMBO journal · 2018Article
- Article
- Calmodulin Lobes Facilitate Dimerization and Activation of Estrogen Receptor-α.The Journal of biological chemistry · 2017Article
- Discovery at the interface: Toward novel anti-proliferative agents targeting human estrogen receptor/S100 interactions.Cell cycle (Georgetown, Tex.) · 2016Article
- Anticipatory UPR Activation: A Protective Pathway and Target in Cancer.Trends in endocrinology and metabolism: TEM · 2016Review
- Estrogen Enhances Linkage in the Vascular Endothelial Calmodulin Network via a Feedforward Mechanism at the G Protein-coupled Estrogen Receptor 1.The Journal of biological chemistry · 2016Article
- In vitro and in vivo effects of tamoxifen against larval stage Echinococcus granulosus.Antimicrobial agents and chemotherapy · 2014Article
- Structural and thermodynamic characterization of the recognition of the S100-binding peptides TRTK12 and p53 by calmodulin.Protein science : a publication of the Protein Society · 2014Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The estrogen receptor α (ER-α) regulates expression of target genes implicated in development, metabolism, and breast cancer. Calcium-dependent regulation of ER-α is critical for activating gene expression and is controlled by calmodulin (CaM). Here, we present the NMR structures for the two lobes of CaM each bound to a localized region of ER-α (residues 287-305). A model of the complete CaM·ER-α complex was constructed by combining these two structures with additional data. The two lobes of CaM both compete for binding at the same site on ER-α (residues 292, 296, 299, 302, and 303), which explains why full-length CaM binds two molecules of ER-α in a 1:2 complex and stabilizes ER-α dimerization. Exposed glutamate residues in CaM (Glu(11), Glu(14), Glu(84), and Glu(87)) form salt bridges with key lysine residues in ER-α (Lys(299), Lys(302), and Lys(303)), which are likely to prevent ubiquitination at these sites and inhibit degradation of ER-α. Mutants of ER-α at the CaM-binding site (W292A and K299A) weaken binding to CaM, and I298E/K299D disrupts estrogen-induced transcription. CaM facilitates dimerization of ER-α in the absence of estrogen, and stimulation of ER-α by either Ca(2+) and/or estrogen may serve to regulate transcription in a combinatorial fashion.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.