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 Communjournal_title
Nature communicationsauthors
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 Tdoi
10.1038/ncomms13021subject
Has Abstractpub_date
2016-10-10 00:00:00pages
13021issn
2041-1723pii
ncomms13021journal_volume
7pub_type
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