Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12897
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Funding
- Austrian Science Funds (FWF) [DKplus W 1226-B18, P 28529-B27]
- Metabolic and Cardiovascular Disease (FWF) at the Medical University of Graz [DKplus W 1226-B18]
- Austrian Academic Exchange Services (OAD)
- Austrian infrastructure programme
- Nikon Austria, Inc.
- BioTechMed
- Bavarian Ministry of Sciences, Research and the Arts (Bavarian Molecular Biosystems Research Network)
- German Research Foundation (Emmy Noether program) [MA 5703/1-1]
- Center for Integrated Protein Science Munich (CIPSM)
- Austrian Science Fund [FWF: P28854]
- Austrian Science Fund (FWF) [P28529, P28854] Funding Source: Austrian Science Fund (FWF)
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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.
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