Journal Article

PUBDB-2022-03945

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png RIM-binding protein couples synaptic vesicle recruitment to release sites

Petzoldt, A. G. ; Götz, T. W. B. ; Driller, J. H. ; Lützkendorf, J. ; Reddy-Alla, S. ; Matkovic-Rachid, T. ; Liu, S.Extern* ; Knoche, E. ; Mertel, S. ; Ugorets, V. ; Lehmann, M. ; Ramesh, N. ; Beuschel, C. B. ; Kuropka, B. ; Freund, C. ; Stelzl, U. ; Loll, B. ; Liu, F. ; Wahl, M. C. ; Sigrist, S. J. (Corresponding author)

2020
Rockefeller Univ. Press New York, NY

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Please use a persistent id in citations: doi:10.1083/jcb.201902059  doi:10.3204/PUBDB-2022-03945

Abstract: 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.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

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Database coverage:
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