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Structure of the endosomal CORVET tethering complex

Author

Listed:
  • Dmitry Shvarev

    (Osnabrück University)

  • Caroline König

    (Osnabrück University)

  • Nicole Susan

    (Osnabrück University)

  • Lars Langemeyer

    (Osnabrück University
    Osnabrück University)

  • Stefan Walter

    (Osnabrück University)

  • Angela Perz

    (Osnabrück University)

  • Florian Fröhlich

    (Osnabrück University
    Osnabrück University)

  • Christian Ungermann

    (Osnabrück University
    Osnabrück University)

  • Arne Moeller

    (Osnabrück University
    Osnabrück University)

Abstract

Cells depend on their endolysosomal system for nutrient uptake and downregulation of plasma membrane proteins. These processes rely on endosomal maturation, which requires multiple membrane fusion steps. Early endosome fusion is promoted by the Rab5 GTPase and its effector, the hexameric CORVET tethering complex, which is homologous to the lysosomal HOPS. How these related complexes recognize their specific target membranes remains entirely elusive. Here, we solve the structure of CORVET by cryo-electron microscopy and revealed its minimal requirements for membrane tethering. As expected, the core of CORVET and HOPS resembles each other. However, the function-defining subunits show marked structural differences. Notably, we discover that unlike HOPS, CORVET depends not only on Rab5 but also on phosphatidylinositol-3-phosphate (PI3P) and membrane lipid packing defects for tethering, implying that an organelle-specific membrane code enables fusion. Our data suggest that both shape and membrane interactions of CORVET and HOPS are conserved in metazoans, thus providing a paradigm how tethering complexes function.

Suggested Citation

  • Dmitry Shvarev & Caroline König & Nicole Susan & Lars Langemeyer & Stefan Walter & Angela Perz & Florian Fröhlich & Christian Ungermann & Arne Moeller, 2024. "Structure of the endosomal CORVET tethering complex," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49137-9
    DOI: 10.1038/s41467-024-49137-9
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    References listed on IDEAS

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    1. Gregory Segala & Marcela A. Bennesch & Nastaran Mohammadi Ghahhari & Deo Prakash Pandey & Pablo C. Echeverria & François Karch & Robert K. Maeda & Didier Picard, 2019. "Vps11 and Vps18 of Vps-C membrane traffic complexes are E3 ubiquitin ligases and fine-tune signalling," Nature Communications, Nature, vol. 10(1), pages 1-15, December.
    2. Joost C.M. Holthuis & Anant K. Menon, 2014. "Lipid landscapes and pipelines in membrane homeostasis," Nature, Nature, vol. 510(7503), pages 48-57, June.
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