RIM-binding protein couples synaptic vesicle recruitment to release sites.

At presynaptic active zones, arrays of large conserved scaffold proteins mediate fast and temporally precise release of synaptic vesicles (SVs). SV release sites could be identified by clusters of Munc13, which allow SVs to dock in defined nanoscale relation to Ca2+ channels. We here show in Drosophila that RIM-binding protein (RIM-BP) connects release sites physically and functionally to the ELKS family Bruchpilot (BRP)-based scaffold engaged in SV recruitment. The RIM-BP N-terminal domain, while dispensable for SV release site organization, was crucial for proper nanoscale patterning of the BRP scaffold and needed for SV recruitment of SVs under strong stimulation. Structural analysis further showed that the RIM-BP fibronectin domains form a "hinge" in the protein center, while the C-terminal SH3 domain tandem binds RIM, Munc13, and Ca2+ channels release machinery collectively. RIM-BPs' conserved domain architecture seemingly provides a relay to guide SVs from membrane far scaffolds into membrane close release sites. © 2020 Petzoldt et al.

Citation

Astrid G Petzoldt, Torsten W B Götz, Jan Heiner Driller, Janine Lützkendorf, Suneel Reddy-Alla, Tanja Matkovic-Rachid, Sunbin Liu, Elena Knoche, Sara Mertel, Vladimir Ugorets, Martin Lehmann, Niraja Ramesh, Christine Brigitte Beuschel, Benno Kuropka, Christian Freund, Ulrich Stelzl, Bernhard Loll, Fan Liu, Markus C Wahl, Stephan J Sigrist. RIM-binding protein couples synaptic vesicle recruitment to release sites. The Journal of cell biology. 2020 Jul 06;219(7)

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PMID: 32369542

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