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<title lang=en>The transcriptional activities and cellular localization of the human estrogen receptor alpha are affected by the synonymous Ala87 mutation.</title>
<creator>Fernández-Calero, Tamara</creator>
<creator>Astrada, Soledad</creator>
<creator>Alberti, Alvaro</creator>
<creator>Horjales, Sofía</creator>
<creator>Arnal, Jean Francois</creator>
<creator>Rovira, Carlos</creator>
<creator>Bollati-Fogolín, Mariela</creator>
<creator>Flouriot, Gilles</creator>
<creator>Marin, Mónica</creator>
<contributor>Biochemistry-Molecular Biology ; Universidad de la Republica-Facultad de Medicina</contributor>
<contributor>Bioinformatics Unit ; Institut Pasteur Montevideo</contributor>
<contributor>Cell Biology Unit ; Institut Pasteur Montevideo</contributor>
<contributor>Institut des Maladies Métaboliques et Cardiovasculaires (I2MC) ; Université Paul Sabatier - Toulouse 3 (UPS) - Hôpital de Rangueil - Institut National de la Santé et de la Recherche Médicale (INSERM)</contributor>
<contributor>Department of Oncology ; Lund University [Lund] - Biomedical Centre (BMC)</contributor>
<contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor>
<description>International audience</description>
<source>Journal of steroid biochemistry and molecular biology </source>
<publisher>Elsevier</publisher>
<identifier>inserm-01015532</identifier>
<identifier>http://www.hal.inserm.fr/inserm-01015532</identifier>
<source>http://www.hal.inserm.fr/inserm-01015532</source>
<source>Journal of steroid biochemistry and molecular biology , Elsevier, 2014, 143C, pp.99-104. 〈10.1016/j.jsbmb.2014.02.016〉</source>
<identifier>DOI : 10.1016/j.jsbmb.2014.02.016</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jsbmb.2014.02.016</relation>
<identifier>PUBMED : 24607813</identifier>
<relation>info:eu-repo/semantics/altIdentifier/pmid/24607813</relation>
<language>en</language>
<subject>[SDV] Life Sciences [q-bio]</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>: Until recently, synonymous mutations (which do not change amino acids) have been much neglected. Some evidence suggests that this kind of mutations could affect mRNA secondary structure or stability, translation kinetics and protein structure. To explore deeper the role of synonymous mutations, we studied their consequence on the functional activity of the estrogen receptor alpha (ERα). The ERα is a ligand-inducible transcription factor that orchestrates pleiotropic cellular effects, at both genomic and non-genomic levels in response to estrogens. In this work we analyzed in transient transfection experiments, the activity of ERα carrying the synonymous mutation Ala87, a polymorphism involving about 5-10% of the population. In comparison to the wild type receptor, our results show that ERαA87 mutation reduces the transactivation efficiency of ERα on an ERE reporter gene while its expression level remains similar. This mutation enhances 4-OHT-induced transactivation of ERα on an AP1 reporter gene. Finally, the mutation affects the subcellular localization of ERα in a cell type specific manner. It enhances the cytoplasmic location of ERα without significant changes in non-genomic effects of E2. The functional alteration of the ERαA87 determined in this work highlights the relevance of synonymous mutations for biomedical and pharmacological points of view.</description>
<date>2014-03-04</date>
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