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. 2009 Jul 13;186(1):129–145. doi: 10.1083/jcb.200812150

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© 2009 Fouquet et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 9. — The N terminus of BRP physically interacts with the C terminus of Cac in vitro. (A) Scheme of yeast two-hybrid analysis using Cac bait constructs and overlapping BRP prey constructs. Full-length Cac protein comprises three large intracellular loops (aa are indicated) and its intracellular C-terminal region (aa 1,420–1,848). The N terminus of BRP (aa 1–320) interacts with the C-terminal region of Cac (83% of the reported cytoplasmic C terminus, sparing the EF hand and most of its IQ motif; Kawasaki et al., 2002). −, no interaction; +++, interaction of high confidence. (B) Co-IPs from Schneider cell extracts cotransfected with a GFP-tagged N-terminal construct of BRP (D1-2^GFP; aa 1–617) and Myc-tagged Cac^C-Term. Western blotting shows the pull-down of the BRP construct in the anti-Myc IP at ∼100 kD (arrow). The corresponding band is not detected in the control lanes (IgGs). The slightly different migration of the band in the input lane and in the IP lanes is the result of differences in sample buffer. MW, molecular weight. (C) Spatiotemporal model of AZ assembly and organization at Drosophila NMJs. SVs, synaptic vesicles.