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

Genny Orso, Diana Pendin, Song Liu, Jessica Tosetto, Tyler J. Moss, Joseph E. Faust, Massimo Micaroni, Anastasia Egorova, Andrea Martinuzzi, James A. McNew () and Andrea Daga ()
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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
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

Nature, 2009, vol. 460, issue 7258, 978-983

Abstract: 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.

Date: 2009
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DOI: 10.1038/nature08280

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