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Cellular metabolism regulates contact sites between vacuoles and mitochondria

Hönscher, C., Mari, M., Auffarth, K., Bohnert, M., Griffith, J., Geerts, W., van der Laan, M., Cabrera, M., Reggiori, F. & Ungermann, C., 14-Jul-2014, In : Developmental Cell. 30, 1, p. 86-94 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

  • Carina Hönscher
  • Muriel Mari
  • Kathrin Auffarth
  • Maria Bohnert
  • Janice Griffith
  • Willie Geerts
  • Martin van der Laan
  • Margarita Cabrera
  • Fulvio Reggiori
  • Christian Ungermann

Emerging evidence suggests that contact sites between different organelles form central hubs in the coordination of cellular physiology. Although recent work has emphasized the crucial role of the endoplasmic reticulum in interorganellar crosstalk, the cooperative behavior of other organelles is largely unexplored. Here, we identify a contact site named vCLAMP (vacuole and mitochondria patch) that integrates mitochondria with the lysosome-like vacuole and thus the endocytic pathway. vCLAMPs depend on the vacuolar HOPS tethering complex subunit Vps39/Vam6 and the Rab GTPase Ypt7, which also participate in membrane fusion at the vacuole. Intriguingly, vCLAMPs are located proximal to the ER-mitochondria encounter structure (ERMES) complexes, and an increase in vCLAMPs can rescue the growth defect of ERMES mutants. Importantly, the persistence of vCLAMPs is regulated by phosphorylation of Vps39 and is strongly reduced during respiratory growth. The identification of this organelle contact site reveals a physical and metabolic interconnection between the endocytic pathway and mitochondria.

Original languageEnglish
Pages (from-to)86-94
Number of pages9
JournalDevelopmental Cell
Volume30
Issue number1
Publication statusPublished - 14-Jul-2014

    Keywords

  • Adaptor Proteins, Vesicular Transport, Biological Transport, Cell Physiological Phenomena, Endoplasmic Reticulum, Membrane Fusion, Microscopy, Electron, Scanning, Microscopy, Fluorescence, Mitochondria, Organelles, Phosphorylation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Vacuoles

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