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The GTPase Rab26 links synaptic vesicles to the autophagy pathway.

MPG-Autoren
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Binotti,  B.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Riedel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Wenzel,  D.
Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society;

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Vorbrüggen,  G.
Research Group of Molecular Cell Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Schalk,  A. M.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Kühnel,  K.
Research Group of Autophagy, MPI for Biophysical Chemistry, Max Planck Society;

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Boyken,  J.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Chua,  J. J. E.
Research Group of Protein Trafficking in Synaptic Development and Function, MPI for Biophysical Chemistry, Max Planck Society;

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Jahn,  R.
Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society;

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Zitation

Binotti, B., Pavlos, N. J., Riedel, D., Wenzel, D., Vorbrüggen, G., Schalk, A. M., et al. (2015). The GTPase Rab26 links synaptic vesicles to the autophagy pathway. eLife, 4: e05597. doi:10.7554/eLife.05597.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0025-02F7-A
Zusammenfassung
Small GTPases of the Rab family not only regulate target recognition in membrane traffic but also control other cellular functions such as cytoskeletal transport and autophagy. Here we show that Rab26 is specifically associated with clusters of synaptic vesicles in neurites. Overexpression of active but not of GDP-preferring Rab26 enhances vesicle clustering, which is particularly conspicuous for the EGFP-tagged variant, resulting in a massive accumulation of synaptic vesicles in neuronal somata without altering the distribution of other organelles. Both endogenous and induced clusters co-localize with autophagy-related proteins such as Atg16L1, LC3B and Rab33B but not with other organelles. Furthermore, Atg16L1 appears to be a direct effector of Rab26 and binds Rab26 in its GTP-bound form, albeit only with low affinity. We propose that Rab26 selectively directs synaptic and secretory vesicles into preautophagosomal structures, suggesting the presence of a novel pathway for degradation of synaptic vesicles.