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Autophagosome–lysosome fusion is independent of V-ATPase-mediated acidification

Author

Listed:
  • Caroline Mauvezin

    (Cell Biology and Development, University of Minnesota)

  • Péter Nagy

    (Cell and Developmental Biology, Eötvös Loránd University)

  • Gábor Juhász

    (Cell and Developmental Biology, Eötvös Loránd University)

  • Thomas P. Neufeld

    (Cell Biology and Development, University of Minnesota)

Abstract

The ATP-dependent proton pump V-ATPase ensures low intralysosomal pH, which is essential for lysosomal hydrolase activity. Based on studies with the V-ATPase inhibitor BafilomycinA1, lysosomal acidification is also thought to be required for fusion with incoming vesicles from the autophagic and endocytic pathways. Here we show that loss of V-ATPase subunits in the Drosophila fat body causes an accumulation of non-functional lysosomes, leading to a block in autophagic flux. However, V-ATPase-deficient lysosomes remain competent to fuse with autophagosomes and endosomes, resulting in a time-dependent formation of giant autolysosomes. In contrast, BafilomycinA1 prevents autophagosome–lysosome fusion in these cells, and this defect is phenocopied by depletion of the Ca2+ pump SERCA, a secondary target of this drug. Moreover, activation of SERCA promotes fusion in a BafilomycinA1-sensitive manner. Collectively, our results indicate that lysosomal acidification is not a prerequisite for fusion, and that BafilomycinA1 inhibits fusion independent of its effect on lysosomal pH.

Suggested Citation

  • Caroline Mauvezin & Péter Nagy & Gábor Juhász & Thomas P. Neufeld, 2015. "Autophagosome–lysosome fusion is independent of V-ATPase-mediated acidification," Nature Communications, Nature, vol. 6(1), pages 1-14, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8007
    DOI: 10.1038/ncomms8007
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    1. Robin Caire & Estelle Audoux & Mireille Thomas & Elisa Dalix & Aurélien Peyron & Killian Rodriguez & Nicola Pordone & Johann Guillemot & Yann Dickerscheit & Hubert Marotte & François Vandenesch & Fréd, 2022. "YAP promotes cell-autonomous immune responses to tackle intracellular Staphylococcus aureus in vitro," Nature Communications, Nature, vol. 13(1), pages 1-19, December.
    2. Vanitha Nithianandam & Hassan Bukhari & Matthew J. Leventhal & Rachel A. Battaglia & Xianjun Dong & Ernest Fraenkel & Mel B. Feany, 2023. "Integrative analysis reveals a conserved role for the amyloid precursor protein in proteostasis during aging," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    3. Keiji Kajiwara & Hiroshi Osaki & Steffen Greßies & Keiko Kuwata & Ju Hyun Kim & Tobias Gensch & Yoshikatsu Sato & Frank Glorius & Shigehiro Yamaguchi & Masayasu Taki, 2022. "A negative-solvatochromic fluorescent probe for visualizing intracellular distributions of fatty acid metabolites," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    4. Joshua J. Rennick & Cameron J. Nowell & Colin W. Pouton & Angus P. R. Johnston, 2022. "Resolving subcellular pH with a quantitative fluorescent lifetime biosensor," Nature Communications, Nature, vol. 13(1), pages 1-13, December.

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