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Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes

Author

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  • Takeshi Ohya

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany)

  • Marta Miaczynska

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany
    Present address: International Institute of Molecular and Cell Biology (IIMCB), Ks. Trojdena 4, 02-109 Warsaw, Poland.)

  • Ünal Coskun

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany)

  • Barbara Lommer

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany)

  • Anja Runge

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany)

  • David Drechsel

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany)

  • Yannis Kalaidzidis

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany
    A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University)

  • Marino Zerial

    (Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01309, Dresden, Germany)

Abstract

Rab GTPases and SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) are evolutionarily conserved essential components of the eukaryotic intracellular transport system. Although pairing of cognate SNAREs is sufficient to fuse membranes in vitro, a complete reconstitution of the Rab–SNARE machinery has never been achieved. Here we report the reconstitution of the early endosomal canine Rab5 GTPase, its key regulators and effectors together with SNAREs into proteoliposomes using a set of 17 recombinant human proteins. These vesicles behave like minimal ‘synthetic’ endosomes, fusing with purified early endosomes or with each other in vitro. Membrane fusion measured by content-mixing and morphological assays requires the cooperativity between Rab5 effectors and cognate SNAREs which, together, form a more efficient ‘core machinery’ than SNAREs alone. In reconstituting a fusion mechanism dependent on both a Rab GTPase and SNAREs, our work shows that the two machineries act coordinately to increase the specificity and efficiency of the membrane tethering and fusion process.

Suggested Citation

  • Takeshi Ohya & Marta Miaczynska & Ünal Coskun & Barbara Lommer & Anja Runge & David Drechsel & Yannis Kalaidzidis & Marino Zerial, 2009. "Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes," Nature, Nature, vol. 459(7250), pages 1091-1097, June.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7250:d:10.1038_nature08107
    DOI: 10.1038/nature08107
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    Cited by:

    1. Seiichi Koike & Reinhard Jahn, 2024. "Rab GTPases and phosphoinositides fine-tune SNAREs dependent targeting specificity of intracellular vesicle traffic," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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