Coimmunoprecipitation experiments were performed as described (Magori & Citovsky, 2011 (link)), with some modifications. Briefly, the tagged proteins were transiently expressed in N. benthamiana leaves after agroinfiltration as described (Lacroix & Citovsky, 2011 (link)), and, after 72 h, infiltrated leaves were harvested and ground into fine powder in liquid nitrogen. Total proteins were extracted from the ground tissues in IP buffer [50 mM Tris-HCl pH 7.5, 150 mM NaCl, 0.1% NP-40, 1 mM EDTA, 3 mM dithiothreitol (DTT), 1× plant protease inhibitor cocktail (Amresco)]. Protein extracts were incubated with anti-GFP antibody (Clontech, dilution 1:250) for 3 hours at 4°C, followed by incubation with Protein G-Sepharose 4B (Invitrogen) for an additional 3 hours at 4°C to capture and precipitate the immune complexes. After three washes with washing buffer (50 mM Tris-HCl pH 7.5, 150 mM NaCl, 0.1% NP-40, and 1 mM EDTA), immunoprecipitates were eluted in SDS sample buffer and subjected to western blot analysis. GFP- and My-tagged proteins were detected by immunoblotting with anti-GFP antibody (Clontech, dilution 1:2000) and anti-cMyc antibody (Genscript, dilution 1:2000), respectively, followed by a secondary antibody conjugated to horseradish peroxidase (ThermoFisher Scientific, dilution 1:2000).