Composition and topology of the endoplasmic reticulum-mitochondria encounter structure
16.09.2011
Stroud DA, Oeljeklaus S, Wiese S, Bohnert M, Lewandrowski U, Sickmann A, Guiard B, van der Laan M, Warscheid B, Wiedemann N
J Mol Biol. 2011 Nov 4;413(4):743-50.
We mapped the glycosylation sites of the endoplasmic reticulum–mitochondria encounter structure (ERMES) and demonstrate that three asparagine residues in the N-terminal domain of Mmm1 are glycosylated. While the glycosylation is dispensable, the cytosolic C-terminal domain of Mmm1 that connects to the Mdm proteins is required for Mmm1 function. To analyze the composition of
ERMES, we determined the subunits by quantitative mass spectrometry.
We identified the calcium-binding GTPase Gem1 as a new ERMES subunit, revealing that ERMES is composed of five genuine subunits. Taken together, ERMES represents a platform that integrates components with functions in formation of ER–mitochondria junctions, maintenance of mitochondrial morphology, protein biogenesis and calcium binding.
