Composition and topology of the endoplasmic reticulum-mitochondria encounter structure.
J Mol Biol
; 413(4): 743-50, 2011 Nov 04.
Article
en En
| MEDLINE
| ID: mdl-21945531
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 Nterminal domain of Mmm1 are glycosylated. While the glycosylation is dispensable, the cytosolic Cterminal 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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Proteínas de Saccharomyces cerevisiae
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Mapeo de Interacción de Proteínas
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Retículo Endoplásmico
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Mitocondrias
Idioma:
En
Revista:
J Mol Biol
Año:
2011
Tipo del documento:
Article
País de afiliación:
Alemania