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  Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation

Ginger, L., Malsam, J., Sonnen, A. F. P., Morado, D., Scheutzow, A., Sollner, T. H., et al. (2020). Arrangements of proteins at reconstituted synaptic vesicle fusion sites depend on membrane separation. Febs Letters, 594(21), 3450-3463. doi:10.1002/1873-3468.13916.

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 Creators:
Ginger, L., Author
Malsam, J., Author
Sonnen, A. F. P., Author
Morado, D., Author
Scheutzow, A., Author
Sollner, T. H., Author
Briggs, John A. G.1, 2, Author              
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              
2European Molecular Biology Laboratory, External Organizations, Heidelberg, DE, ou_3346677              

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Free keywords: cryoelectron tomography fusion in vitroreconstitution membrane SNARE synaptic vesicle neurotransmitter release molecular-mechanisms docked vesicles snare complexes synaptotagmin-i machinery munc18-1 hypothesis template binding Biochemistry & Molecular Biology Biophysics Cell Biology
 Abstract: Synaptic vesicle proteins, including N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs), Synaptotagmin-1 and Complexin, are responsible for controlling the synchronised fusion of synaptic vesicles with the presynaptic plasma membrane in response to elevated cytosolic calcium levels. A range of structures of SNAREs and their regulatory proteins have been elucidated, but the exact organisation of these proteins at synaptic junction membranes remains elusive. Here, we have used cryoelectron tomography to investigate the arrangement of synaptic proteins in anin vitroreconstituted fusion system. We found that the separation between vesicle and target membranes strongly correlates with the organisation of protein complexes at junctions. At larger membrane separations, protein complexes assume a 'clustered' distribution at the docking site, inducing a protrusion in the target membrane. As the membrane separation decreases, protein complexes become displaced radially outwards and assume a 'ring-like' arrangement. Our findings indicate that docked vesicles can possess a wide range of protein complex numbers and be heterogeneous in their protein arrangements.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000568434100001
DOI: 10.1002/1873-3468.13916
ISSN: 0014-5793
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Title: Febs Letters
  Alternative Title : FEBS Lett.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 594 (21) Sequence Number: - Start / End Page: 3450 - 3463 Identifier: -