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

MPG-Autoren
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Göttfert,  F.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

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Kamin,  D.
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

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Hell,  S. W.       
Department of NanoBiophotonics, MPI for Biophysical Chemistry, Max Planck Society;

Externe Ressourcen

http://elifesciences.org/content/4/e06935.full.pdf
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Zitation

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.06935.001.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0028-3A0F-1
Zusammenfassung
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.