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Homotypic fusion of ER membranes requires the dynamin-like GTPase Atlastin

Author

Listed:
  • Genny Orso

    (Eugenio Medea Scientific Institute)

  • Diana Pendin

    (Eugenio Medea Scientific Institute)

  • Song Liu

    (Rice University, Houston, Texas 77005, USA)

  • Jessica Tosetto

    (Eugenio Medea Scientific Institute
    University of Padova)

  • Tyler J. Moss

    (Rice University, Houston, Texas 77005, USA)

  • Joseph E. Faust

    (Rice University, Houston, Texas 77005, USA)

  • Massimo Micaroni

    (University of Queensland, Institute for Molecular Bioscience, St Lucia, Brisbane, Queensland 4072, Australia)

  • Anastasia Egorova

    (Consorzio “Mario Negri Sud”, Santa Maria Imbaro 66030, Italy)

  • Andrea Martinuzzi

    (Eugenio Medea Scientific Institute)

  • James A. McNew

    (Rice University, Houston, Texas 77005, USA)

  • Andrea Daga

    (Eugenio Medea Scientific Institute
    Dulbecco Telethon Institute, Eugenio Medea Scientific Institute
    The David Geffen School of Medicine, University of California, Los Angeles, California 90095, USA)

Abstract

Establishment and maintenance of proper architecture is essential for endoplasmic reticulum (ER) function. Homotypic membrane fusion is required for ER biogenesis and maintenance, and has been shown to depend on GTP hydrolysis. Here we demonstrate that Drosophila Atlastin—the fly homologue of the mammalian GTPase atlastin 1 involved in hereditary spastic paraplegia—localizes on ER membranes and that its loss causes ER fragmentation. Drosophila Atlastin embedded in distinct membranes has the ability to form trans-oligomeric complexes and its overexpression induces enlargement of ER profiles, consistent with excessive fusion of ER membranes. In vitro experiments confirm that Atlastin autonomously drives membrane fusion in a GTP-dependent fashion. In contrast, GTPase-deficient Atlastin is inactive, unable to form trans-oligomeric complexes owing to failure to self-associate, and incapable of promoting fusion in vitro. These results demonstrate that Atlastin mediates membrane tethering and fusion and strongly suggest that it is the GTPase activity that is required for ER homotypic fusion.

Suggested Citation

  • Genny Orso & Diana Pendin & Song Liu & Jessica Tosetto & Tyler J. Moss & Joseph E. Faust & Massimo Micaroni & Anastasia Egorova & Andrea Martinuzzi & James A. McNew & Andrea Daga, 2009. "Homotypic fusion of ER membranes requires the dynamin-like GTPase Atlastin," Nature, Nature, vol. 460(7258), pages 978-983, August.
    • Handle: RePEc:nat:nature:v:460:y:2009:i:7258:d:10.1038_nature08280
    DOI: 10.1038/nature08280
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    Cited by:

    1. Patrick A. Sandoz & Robin A. Denhardt-Eriksson & Laurence Abrami & Luciano A. Abriata & Gard Spreemann & Catherine Maclachlan & Sylvia Ho & Béatrice Kunz & Kathryn Hess & Graham Knott & Francisco S. M, 2023. "Dynamics of CLIMP-63 S-acylation control ER morphology," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    2. Lijun Shi & Chenguang Yang & Mingyuan Zhang & Kangning Li & Keying Wang & Li Jiao & Ruming Liu & Yunyun Wang & Ming Li & Yong Wang & Lu Ma & Shuxin Hu & Xin Bian, 2024. "Dissecting the mechanism of atlastin-mediated homotypic membrane fusion at the single-molecule level," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Yoko Shibata & Emily E. Mazur & Buyan Pan & Joao A. Paulo & Steven P. Gygi & Suyog Chavan & L. Sebastian Alexis Valerio & Jiuchun Zhang & Tom A. Rapoport, 2024. "The membrane curvature-inducing REEP1-4 proteins generate an ER-derived vesicular compartment," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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