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  The GTPase Rab26 links synaptic vesicles to the autophagy pathway.

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-02F7-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-6DC8-B
Genre: Journal Article

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 Creators:
Binotti, B.1, Author              
Pavlos, N. J., Author
Riedel, D.2, Author              
Wenzel, D.2, Author              
Vorbrüggen, G.3, Author              
Schalk, A. M.1, Author              
Kühnel, K.4, Author              
Boyken, J.1, Author              
Erck, C., Author
Martens, H., Author
Chua, J. J. E.5, Author              
Jahn, R.1, Author              
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              
3Research Group of Molecular Cell Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578593              
4Research Group of Autophagy, MPI for Biophysical Chemistry, Max Planck Society, ou_1933285              
5Research Group of Protein Trafficking in Synaptic Development and Function, MPI for Biophysical Chemistry, Max Planck Society, ou_1933287              

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 Abstract: 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.

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Language(s): eng - English
 Dates: 2015-02-02
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.05597
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Title: eLife
Source Genre: Journal
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Pages: 23 Volume / Issue: 4 Sequence Number: e05597 Start / End Page: - Identifier: -