A dynamic interface between vacuoles and mitochondria in yeast.
Cellular life depends on continuous transport of lipids and small molecules between mitochondria and the endomembrane system. Recently, endoplasmic reticulum-mitochondrial encounter structure (ERMES) was identified as an important yet nonessential contact for such transport. Using a high-content screen in yeast, we found a contact site, marked by Vam6/Vps39, between vacuoles (the yeast ... lysosomal compartment) and mitochondria, named vCLAMP (vacuole and mitochondria patch). vCLAMP is enriched with ion and amino-acid transporters and has a role in lipid relay between the endomembrane system and mitochondria. Critically, we show that mitochondria are dependent on having one of two contact sites, ERMES or vCLAMP. The absence of one causes expansion of the other, and elimination of both is lethal. Identification of vCLAMP adds to our ability to understand the complexity of interorganellar crosstalk.
Mesh Terms:
Adaptor Proteins, Vesicular Transport, Biological Transport, Cell Physiological Phenomena, Chromatography, Liquid, Endoplasmic Reticulum, Immunoprecipitation, Membrane Fusion, Microscopy, Electron, Scanning, Microscopy, Fluorescence, Mitochondria, Phospholipids, Phosphorylation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Vacuoles
Adaptor Proteins, Vesicular Transport, Biological Transport, Cell Physiological Phenomena, Chromatography, Liquid, Endoplasmic Reticulum, Immunoprecipitation, Membrane Fusion, Microscopy, Electron, Scanning, Microscopy, Fluorescence, Mitochondria, Phospholipids, Phosphorylation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Vacuoles
Dev. Cell
Date: Jul. 14, 2014
PubMed ID: 25026036
View in: Pubmed Google Scholar
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