Membrane association of estrogen receptor alpha and beta influences 17beta-estradiol-mediated cancer cell proliferation.

Steroids
Maria Marino, Paolo Ascenzi

Abstract

S-Palmitoylation is a widespread post-translational modification of integral and/or peripheral proteins occurring in all eukaryotic cells. The family of S-palmitoylated proteins is large and diverse and recently, estrogen receptor isoforms (ERalpha and ERbeta) belonging to the nuclear receptor superfamily have been added to the palmitoylproteoma. S-Palmitoylation allows ERalpha and ERbeta localization at the plasma membrane, where they associate with caveolin-1. Upon 17beta-estradiol (E2) stimulation, ERalpha dissociates from caveolin-1 allowing the activation of rapid signals relevant for cell proliferation. In contrast to ERalpha, E2 increases ERbeta association with caveolin-1 and activates p38 kinase and the downstream pro-apoptotic cascade (i.e., caspase-3 activation and PARP cleavage). These data highlight the physiological role of palmitoylation in modulating the ERalpha and ERbeta localization at the plasma membrane and the regulation of different E2-induced non-genomic functions relevant for controlling cell proliferation.

Citations

Oct 10, 2014·Cell Death & Disease·M FiocchettiM Marino
Apr 22, 2015·Seminars in Cancer Biology·Mark A FeitelsonSomaira Nowsheen
Mar 2, 2011·Molecular Aspects of Medicine·Maria MarinoFlavia Franconi
May 12, 2009·Molecular Aspects of Medicine·Alessandra di MasiMaria Marino
Dec 18, 2015·Médecine sciences : M/S·Marine AdlanmeriniJean-François Arnal
Jun 25, 2009·Molecular and Cellular Endocrinology·Gabriella CastoriaFerdinando Auricchio
Sep 23, 2008·Biochimica Et Biophysica Acta·Marinella ZilliUNKNOWN Consorzio Interuniversitario Nazionale per la Bio-Oncologia (CINBO)
Apr 29, 2015·Molecular and Cellular Endocrinology·Zhao-Yi Wang, Li Yin
Jun 27, 2015·Biochimica Et Biophysica Acta·Marc Yeste-VelascoYong-Jie Lu
Jun 15, 2010·Immunology Letters·Marina PierdominiciElena Ortona
Jan 8, 2016·Dose-response : a Publication of International Hormesis Society·Filippo AcconciaMaria Marino
Jan 25, 2013·International Journal of Molecular Sciences·Rocío García-BecerraJavier Camacho
Aug 12, 2009·Cellular and Molecular Life Sciences : CMLS·Elin SwedenborgJoëlle Rüegg
Jun 18, 2011·Endocrine Reviews·Muriel Le RomancerLaura Corbo
Jun 24, 2020·International Journal of Molecular Sciences·Jin BaiDong-Bao Chen
Dec 11, 2013·Translational Stroke Research·Ami P RavalHelen Bramlett
May 26, 2017·Physiological Reviews·Jean-Francois ArnalJohn Katzenellenbogen
Dec 21, 2017·Reproductive Medicine and Biology·Pelin YaşarMesut Muyan
Aug 28, 2020·Frontiers in Endocrinology·Maria Teresa PaganoMaria Luisa Dupuis
Feb 5, 2015·Cancer Epidemiology, Biomarkers & Prevention : a Publication of the American Association for Cancer Research, Cosponsored by the American Society of Preventive Oncology·Lori S TillmansPaul J Limburg
Nov 17, 2020·Frontiers in Oncology·Rahul MalMathew A Cherian
Mar 10, 2019·The Journal of Steroid Biochemistry and Molecular Biology·Priya BhardwajKristy A Brown
Aug 4, 2021·Reproductive Toxicology·Thalles Fernando Rocha RuizEllen Cristina Rivas Leonel

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