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Gottschalk, B; Klec, C; Leitinger, G; Bernhart, E; Rost, R; Bischof, H; Madreiter-Sokolowski, CT; Radulović, S; Eroglu, E; Sattler, W; Waldeck-Weiermair, M; Malli, R; Graier, WF.
MICU1 controls cristae junction and spatially anchors mitochondrial Ca2+ uniporter complex.
Nat Commun. 2019; 10(1):3732-3732
Doi: 10.1038/s41467-019-11692-x
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- Führende Autor*innen der Med Uni Graz
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Gottschalk Benjamin
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Graier Wolfgang
- Co-Autor*innen der Med Uni Graz
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Bernhart Eva Maria
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Bischof Helmut
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EROGLU Emrah
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Klec Christiane
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Leitinger Gerd
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Madreiter-Sokolowski Corina
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Malli Roland
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Radulovic Snjezana
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Rost René
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Sattler Wolfgang
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Waldeck-Weiermair Markus
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- Abstract:
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Recently identified core proteins (MICU1, MCU, EMRE) forming the mitochondrial Ca2+ uniporter complex propelled investigations into its physiological workings. Here, we apply structured illumination microscopy to visualize and localize these proteins in living cells. Our data show that MICU1 localizes at the inner boundary membrane (IBM) due to electrostatic interaction of its polybasic domain. Moreover, this exclusive localization of MICU1 is important for the stability of cristae junctions (CJ), cytochrome c release and mitochondrial membrane potential. In contrast to MICU1, MCU and EMRE are homogeneously distributed at the inner mitochondrial membrane under resting conditions. However, upon Ca2+ elevation MCU and EMRE dynamically accumulate at the IBM in a MICU1-dependent manner. Eventually, our findings unveil an essential function of MICU1 in CJ stabilization and provide mechanistic insights of how sophistically MICU1 controls the MCU-Complex while maintaining the structural mitochondrial membrane framework.
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