Details

Autor(en) / Beteiligte

• Ellenrieder, Lars
• Opaliński, Łukasz
• Becker, Lars
• Krüger, Vivien
• Mirus, Oliver
• Straub, Sebastian P
• Ebell, Katharina
• Flinner, Nadine
• Stiller, Sebastian B
• Guiard, Bernard
• Meisinger, Chris
• Wiedemann, Nils
• Schleiff, Enrico
• Wagner, Richard
• Pfanner, Nikolaus
• Becker, Thomas

Titel

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

Ist Teil von

• Nature communications, 2016-10, Vol.7 (1), p.13021-13021, Article 13021

Ort / Verlag

England: Nature Publishing Group

Erscheinungsjahr

2016

Link zum Volltext

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• 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.