Separating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10

Lars Ellenrieder, Łukasz Opaliński, Lars Becker, Vivien Krüger, Oliver Mirus, Sebastian P. Straub, Katharina Ebell, Nadine Flinner, Sebastian B. Stiller, Bernard Guiard, Chris Meisinger, Nils Wiedemann, Enrico Schleiff, Richard Wagner, Nikolaus Pfanner () and Thomas Becker ()
Additional contact information
Lars Ellenrieder: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Łukasz Opaliński: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Lars Becker: School of Biology/Chemistry, University of Osnabrück
Vivien Krüger: School of Biology/Chemistry, University of Osnabrück
Oliver Mirus: Molecular Cell Biology of Plants, University of Frankfurt
Sebastian P. Straub: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Katharina Ebell: School of Biology/Chemistry, University of Osnabrück
Nadine Flinner: Molecular Cell Biology of Plants, University of Frankfurt
Sebastian B. Stiller: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Bernard Guiard: Centre de Génétique Moléculaire, Centre National de la Recherche Scientifique
Chris Meisinger: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Nils Wiedemann: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Enrico Schleiff: Molecular Cell Biology of Plants, University of Frankfurt
Richard Wagner: School of Biology/Chemistry, University of Osnabrück
Nikolaus Pfanner: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg
Thomas Becker: Institute of Biochemistry and Molecular Biology, Centre for Biochemistry and Molecular Cell Research, Faculty of Medicine, University of Freiburg

Nature Communications, 2016, vol. 7, issue 1, 1-14

Abstract: Abstract The endoplasmic reticulum–mitochondria encounter structure (ERMES) connects the mitochondrial outer membrane with the ER. Multiple functions have been linked to ERMES, including maintenance of mitochondrial morphology, protein assembly and phospholipid homeostasis. Since the mitochondrial distribution and morphology protein Mdm10 is present in both ERMES and the mitochondrial sorting and assembly machinery (SAM), it is unknown how the ERMES functions are connected on a molecular level. Here we report that conserved surface areas on opposite sides of the Mdm10 β-barrel interact with SAM and ERMES, respectively. We generated point mutants to separate protein assembly (SAM) from morphology and phospholipid homeostasis (ERMES). Our study reveals that the β-barrel channel of Mdm10 serves different functions. Mdm10 promotes the biogenesis of α-helical and β-barrel proteins at SAM and functions as integral membrane anchor of ERMES, demonstrating that SAM-mediated protein assembly is distinct from ER-mitochondria contact sites.

Date: 2016
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/ncomms13021 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:7:y:2016:i:1:d:10.1038_ncomms13021

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

DOI: 10.1038/ncomms13021

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 ().