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Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid

Madreiter-Sokolowski, CT; Klec, C; Parichatikanond, W; Stryeck, S; Gottschalk, B; Pulido, S; Rost, R; Eroglu, E; Hofmann, NA; Bondarenko, AI; Madl, T; Waldeck-Weiermair, M; Malli, R; Graier, WF.
PRMT1-mediated methylation of MICU1 determines the UCP2/3 dependency of mitochondrial Ca(2+) uptake in immortalized cells.
Nat Commun. 2016; 7: 12897-12897. [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG

 

Autor/innen der Med Uni Graz:
Bondarenko Oleksandr
Eroglu Emrah
Gottschalk Benjamin
Graier Wolfgang
Hofmann Nicole
Klec Christiane
Madl Tobias
Madreiter-Sokolowski Corina
Malli Roland
Parichatikanond Warisara
Rost René
Stryeck Sarah
Waldeck-Weiermair Markus
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Number of Figures: 6
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Abstract:
Recent studies revealed that mitochondrial Ca(2+) channels, which control energy flow, cell signalling and death, are macromolecular complexes that basically consist of the pore-forming mitochondrial Ca(2+) uniporter (MCU) protein, the essential MCU regulator (EMRE), and the mitochondrial Ca(2+) uptake 1 (MICU1). MICU1 is a regulatory subunit that shields mitochondria from Ca(2+) 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 Ca(2+) uptake. Here we clarify the molecular mechanism that determines the UCP2/3 dependency of mitochondrial Ca(2+) uptake. Our data demonstrate that mitochondrial Ca(2+) uptake is controlled by protein arginine methyl transferase 1 (PRMT1) that asymmetrically methylates MICU1, resulting in decreased Ca(2+) sensitivity. UCP2/3 normalize Ca(2+) sensitivity of methylated MICU1 and, thus, re-establish mitochondrial Ca(2+) uptake activity. These data provide novel insights in the complex regulation of the mitochondrial Ca(2+) uniporter by PRMT1 and UCP2/3.

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