MICU1 controls cristae junction and spatially anchors mitochondrial Ca2+ uniporter complex

Benjamin Gottschalk, Christiane Klec, Gerd Leitinger, Eva Bernhart, René Rost, Helmut Bischof, Corina T. Madreiter-Sokolowski, Snježana Radulović, Emrah Eroglu, Wolfgang Sattler, Markus Waldeck-Weiermair, Roland Malli and Wolfgang F. Graier ()
Additional contact information
Benjamin Gottschalk: Medical University of Graz
Christiane Klec: Medical University of Graz
Gerd Leitinger: Medical University of Graz
Eva Bernhart: Medical University of Graz
René Rost: Medical University of Graz
Helmut Bischof: Medical University of Graz
Corina T. Madreiter-Sokolowski: Medical University of Graz
Snježana Radulović: Medical University of Graz
Emrah Eroglu: Medical University of Graz
Wolfgang Sattler: Medical University of Graz
Markus Waldeck-Weiermair: Medical University of Graz
Roland Malli: Medical University of Graz
Wolfgang F. Graier: Medical University of Graz

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract 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.

Date: 2019
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-019-11692-x Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11692-x

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-11692-x

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().