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. 2013 May 15;24(10):1593–1601. doi: 10.1091/mbc.E13-02-0074

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© 2013 El Kasmi et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 3: — Interaction analysis of candidate SNARE proteins involved in cytokinesis. GFP-KNOLLE (A), YFP-NPSN11 (B), Myc-SNAP33 (C), and Myc-VAMP721 (D) were immunoprecipitated from total protein extracts of Arabidopsis inflorescences. (A) GFP-KNOLLE coprecipitated SYP71 and R-SNAREs VAMP721 and VAMP722. (B) YFP-NPSN11 coprecipitated SYP71 and R-SNAREs VAMP721 and VAMP722. (C) Myc-SNAP33 coprecipitated R-SNAREs VAMP721 and VAMP722 but not SYP71 (arrow). The upper band in (T) and (FT) represents a protein that cross-reacted with the SNAP33 antiserum and was not precipitated. (D) Myc-VAMP721 coprecipitated KNOLLE and NPSN11. Protein was detected in total extract (T), flowthrough (FT), and immunoprecipitate (IP) by Western blot using anti-SNAP33 (S33), anti-NPSN11 (N11), anti-KNOLLE (KN), anti-SYP71 (S71), or anti-VAMP721/722 (V721/722) antiserum. Note that there is no interaction of endogenous KNOLLE, NPSN11, SNAP33, or VAMP721/722 with their GFP-, YFP-, or Myc-tagged fusion protein; the immunoblots show only GFP-KNOLLE, YFP-NPSN11, Myc-SNAP33, and Myc-VAMP721/722, as indicated by the molecular weight (in kilodaltons) on the right side.