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

MPG-Autoren
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Ohya,  Takeshi
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Miaczynska,  Marta
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Lommer,  Barbara
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Runge,  Anja
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Drechsel,  David
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Kalaidzidis,  Yannis
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Zerial,  Marino
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Zitation

Ohya, T., Miaczynska, M., Coskun, Ü., Lommer, B., Runge, A., Drechsel, D., et al. (2009). Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes. Nature, 459(7250), 1091-1097.


Zitierlink: http://hdl.handle.net/21.11116/0000-0001-0D6E-7
Zusammenfassung
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.