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

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Ellenrieder L,Opaliński Ł,Becker L,Krüger V,Mirus O,Straub SP,Ebell K,Flinner N,Stiller SB,Guiard B,Meisinger C,Wiedemann N,Schleiff E,Wagner R,Pfanner N,Becker T

doi

10.1038/ncomms13021

subject

Has Abstract

pub_date

2016-10-10 00:00:00

pages

13021

issn

2041-1723

pii

ncomms13021

journal_volume

7

pub_type

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