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  A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones

Siebert, M., Böhme, M. A., Driller, J. H., Babikir, H., Mampell, M. M., Rey, U., et al. (2015). A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones. eLife, 4: e06935. doi:10.7554/eLife.06935.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-4B35-B Version Permalink: http://hdl.handle.net/21.11116/0000-0002-7997-C
Genre: Journal Article

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 Creators:
Siebert, Matthias1, Author
Böhme, Mathias A1, Author
Driller, Jan H1, Author
Babikir, Husam1, Author
Mampell, Malou M1, Author
Rey, Ulises2, Author              
Ramesh, Niraja1, Author
Matkovic, Tanja1, Author
Holton, Nicole1, Author
Reddy-Alla, Suneel1, Author
Göttfert, Fabian1, Author
Kamin, Dirk1, Author
Quentin, Christine1, Author
Klinedinst, Susan1, Author
Andlauer, Till FM1, Author
Hell, Stefan W1, Author
Collins, Catherine A1, Author
Wahl, Markus C1, Author
Loll, Bernhard1, Author
Sigrist, Stephan J1, Author
Affiliations:
1external, ou_persistent22              
2Reinhard Lipowsky, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863327              

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Free keywords: Open Access
 Abstract: Synaptic vesicles (SVs) fuse at active zones (AZs) covered by a protein scaffold, at Drosophila synapses comprised of ELKS family member Bruchpilot (BRP) and RIM-binding protein (RBP). We here demonstrate axonal co-transport of BRP and RBP using intravital live imaging, with both proteins co-accumulating in axonal aggregates of several transport mutants. RBP, via its C-terminal Src-homology 3 (SH3) domains, binds Aplip1/JIP1, a transport adaptor involved in kinesin-dependent SV transport. We show in atomic detail that RBP C-terminal SH3 domains bind a proline-rich (PxxP) motif of Aplip1/JIP1 with submicromolar affinity. Pointmutating this PxxP motif provoked formation of ectopic AZ-like structures at axonal membranes. Direct interactions between AZ proteins and transport adaptors seem to provide complex avidity and shield synaptic interaction surfaces of pre-assembled scaffold protein transport complexes, thus, favouring physiological synaptic AZ assembly over premature assembly at axonal membranes. DOI: http://dx.doi.org/10.7554/eLife.06935.001 Author keywordsResearch organism

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 Dates: 2015-08-142015
 Publication Status: Published in print
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 Identifiers: DOI: 10.7554/eLife.06935
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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 4 Sequence Number: e06935 Start / End Page: - Identifier: ISSN: 2050-084X