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Title: PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca<sup>2+</sup> uptake in immortalized cells
Authors: Corina T. Madreiter-Sokolowski
Christiane Klec
Warisara Parichatikanond
Sarah Stryeck
Benjamin Gottschalk
Sergio Pulido
Rene Rost
Emrah Eroglu
Nicole A. Hofmann
Alexander I. Bondarenko
Tobias Madl
Markus Waldeck-Weiermair
Roland Malli
Wolfgang F. Graier
Medizinische Universitat Graz
Karl-Franzens-Universitat Graz
Technical University of Munich
Helmholtz Center Munich German Research Center for Environmental Health
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology;Chemistry
Issue Date: 19-Sep-2016
Citation: Nature Communications. Vol.7, (2016)
Abstract: © 2016 The Author(s). Recent studies revealed that mitochondrial Ca2+ channels, which control energy flow, cell signalling and death, are macromolecular complexes that basically consist of the pore-forming mitochondrial Ca2+ uniporter (MCU) protein, the essential MCU regulator (EMRE), and the mitochondrial Ca2+ uptake 1 (MICU1). MICU1 is a regulatory subunit that shields mitochondria from Ca2+ overload. Before the identification of these core elements, the novel uncoupling proteins 2 and 3 (UCP2/3) have been shown to be fundamental for mitochondrial Ca2+ uptake. Here we clarify the molecular mechanism that determines the UCP2/3 dependency of mitochondrial Ca2+ uptake. Our data demonstrate that mitochondrial Ca2+ uptake is controlled by protein arginine methyl transferase 1 (PRMT1) that asymmetrically methylates MICU1, resulting in decreased Ca2+ sensitivity. UCP2/3 normalize Ca2+ sensitivity of methylated MICU1 and, thus, re-establish mitochondrial Ca2+ uptake activity. These data provide novel insights in the complex regulation of the mitochondrial Ca2+ uniporter by PRMT1 and UCP2/3.
ISSN: 20411723
Appears in Collections:Scopus 2016-2017

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