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.; Ramesh, N.; Matkovic, T.; Holton, N.; Reddy-Alla, S.; Göttfert, F.; Kamin, D.; Quentin, C.; Klinedinst, S.; Andlauer, T. F.; Hell, S. W.; Collins, C. A.; Wahl, M. C.; Loll, B.; Sigrist, S. J.

doi:10.7554/eLife.06935.001

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学術論文

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

MPS-Authors

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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;

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引用

Siebert, M., Böhme, M. A., Driller, J. H., Babikir, H., Mampell, M. M., Rey, U., Ramesh, N., Matkovic, T., Holton, N., Reddy-Alla, S., Göttfert, F., Kamin, D., Quentin, C., Klinedinst, S., Andlauer, T. F., Hell, S. W., Collins, C. A., Wahl, M. C., Loll, B., & Sigrist, S. J. (2015). A high affinity RIM-binding protein/Aplip1 interaction prevents the formation of ectopic axonal active zones. eLife, 4:. doi:10.7554/eLife.06935.001.

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

要旨

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.