Eukaryotic cells contain multiple organelles, which are functionally and structurally interconnected. The endoplasmic reticulum-mitochondria encounter structure (ERMES) forms a junction between mitochondria and the endoplasmic reticulum (ER). Four ERMES proteins are known in yeast, the ER-anchored protein Mmm1 and three mitochondria-associated proteins, Mdm10, Mdm12 and Mdm34, with functions related to mitochondrial morphology and protein biogenesis. We mapped the glycosylation sites of 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.
%0 Journal Article
%1 stroudCompositionTopologyEndoplasmic2011
%A Stroud, David A.
%A Oeljeklaus, Silke
%A Wiese, Sebastian
%A Bohnert, Maria
%A Lewandrowski, Urs
%A Sickmann, Albert
%A Guiard, Bernard
%A van der Laan, Martin
%A Warscheid, Bettina
%A Wiedemann, Nils
%C Netherlands
%D 2011
%J Journal of molecular biology
%K *Protein Biological,Models Chemical,Protein Interaction Mapping,Endoplasmic Multimerization,Protein Proteins/chemistry/*metabolism,Saccharomyces Reticulum/chemistry/*metabolism,Glycosylation,Mass Spectrometry,Mitochondria/chemistry/*metabolism,Models Subunits/analysis,Saccharomyces cerevisiae cerevisiae/chemistry/*cytology/*metabolism,to_read
%N 4
%P 743--750
%R 10.1016/j.jmb.2011.09.012
%T Composition and Topology of the Endoplasmic Reticulum-Mitochondria Encounter Structure.
%V 413
%X Eukaryotic cells contain multiple organelles, which are functionally and structurally interconnected. The endoplasmic reticulum-mitochondria encounter structure (ERMES) forms a junction between mitochondria and the endoplasmic reticulum (ER). Four ERMES proteins are known in yeast, the ER-anchored protein Mmm1 and three mitochondria-associated proteins, Mdm10, Mdm12 and Mdm34, with functions related to mitochondrial morphology and protein biogenesis. We mapped the glycosylation sites of 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.
@article{stroudCompositionTopologyEndoplasmic2011,
abstract = {Eukaryotic cells contain multiple organelles, which are functionally and structurally interconnected. The endoplasmic reticulum-mitochondria encounter structure (ERMES) forms a junction between mitochondria and the endoplasmic reticulum (ER). Four ERMES proteins are known in yeast, the ER-anchored protein Mmm1 and three mitochondria-associated proteins, Mdm10, Mdm12 and Mdm34, with functions related to mitochondrial morphology and protein biogenesis. We mapped the glycosylation sites of 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.},
added-at = {2024-05-17T13:01:35.000+0200},
address = {Netherlands},
author = {Stroud, David A. and Oeljeklaus, Silke and Wiese, Sebastian and Bohnert, Maria and Lewandrowski, Urs and Sickmann, Albert and Guiard, Bernard and {van der Laan}, Martin and Warscheid, Bettina and Wiedemann, Nils},
biburl = {https://www.bibsonomy.org/bibtex/2e32d6c000874884f5cab121bfdfcfa1b/warscheidlab},
copyright = {Copyright {\copyright} 2011 Elsevier Ltd. All rights reserved.},
doi = {10.1016/j.jmb.2011.09.012},
interhash = {579225108b8d3c43fbbdcdba9147aca4},
intrahash = {e32d6c000874884f5cab121bfdfcfa1b},
issn = {1089-8638 0022-2836},
journal = {Journal of molecular biology},
keywords = {*Protein Biological,Models Chemical,Protein Interaction Mapping,Endoplasmic Multimerization,Protein Proteins/chemistry/*metabolism,Saccharomyces Reticulum/chemistry/*metabolism,Glycosylation,Mass Spectrometry,Mitochondria/chemistry/*metabolism,Models Subunits/analysis,Saccharomyces cerevisiae cerevisiae/chemistry/*cytology/*metabolism,to_read},
langid = {english},
month = nov,
number = 4,
pages = {743--750},
pmid = {21945531},
timestamp = {2024-05-17T13:01:35.000+0200},
title = {Composition and Topology of the Endoplasmic Reticulum-Mitochondria Encounter Structure.},
volume = 413,
year = 2011
}