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Journal Article

SNAREs define targeting specificity of trafficking vesicles by combinatorial interaction with tethering factors.

MPS-Authors
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Koike,  S.
Department of Neurobiology, 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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Fulltext (public)

3047325.pdf
(Publisher version), 6MB

Supplementary Material (public)

3047325_Suppl_1.pdf
(Supplementary material), 7MB

3047325_Suppl_2.pdf
(Supplementary material), 185KB

3047325_Suppl_3.pdf
(Supplementary material), 86KB

Citation

Koike, S., & Jahn, R. (2019). SNAREs define targeting specificity of trafficking vesicles by combinatorial interaction with tethering factors. Nature Communicationsvolume, 10: 1608. doi:10.1038/s41467-019-09617-9.


Cite as: https://hdl.handle.net/21.11116/0000-0003-5FA0-E
Abstract
Membrane traffic operates by vesicles that bud from precursor organelles and are transported to their target compartment where they dock and fuse. Targeting requires tethering factors recruited by small GTPases and phosphoinositides whereas fusion is carried out by SNARE proteins. Here we report that vesicles containing the Q-SNAREs syntaxin 13 (Stx13) and syntaxin 6 (Stx6) together are targeted to a different endosomal compartment than vesicles containing only Stx6 using injection of artificial vesicles. Targeting by Stx6 requires Vps51, a component of the GARP/EARP tethering complexes. In contrast, targeting by both Stx6 and Stx13 is governed by Vps13B identified here as tethering factor functioning in transport from early endosomes to recycling endosomes. Vps13B specifically binds to Stx13/Stx6 as well as to Rab14, Rab6, and PtdIns(3)P. We conclude that SNAREs use a combinatorial code for recruiting tethering factors, revealing a key function in targeting that is independent of SNARE pairing during fusion.