Laboratory of Cell Biology, Institute of Experimental Botany, Czech Academy of Sciences, Rozvojová 263, 165 02, Prague 6, Czech Republic.
Laboratory of Cell Morphogenesis, Department of Experimental Plant Biology, Charles University in Prague, Faculty of Science, Viničná 5, 128 44, Prague 2, Czech Republic.
J Exp Bot. 2022 Jan 27;73(3):742-755. doi: 10.1093/jxb/erab457.
In the reaction to non-adapted Blumeria graminis f. sp. hordei (Bgh), Arabidopsis thaliana leaf epidermal cells deposit cell wall reinforcements called papillae or seal fungal haustoria in encasements, both of which involve intensive exocytosis. A plant syntaxin, SYP121/PEN1, has been found to be of key importance for the timely formation of papillae, and the vesicle tethering complex exocyst subunit EXO70B2 has been found to contribute to their morphology. Here, we identify a specific role for the EXO70B2-containing exocyst complex in the papillae membrane domains important for callose deposition and GFP-SYP121 delivery to the focal attack sites, as well as its contribution to encasement formation. The mRuby2-EXO70B2 co-localizes with the exocyst core subunit SEC6 and GFP-SYP121 in the membrane domain of papillae, and EXO70B2 and SYP121 proteins have the capacity to directly interact. The exo70B2/syp121 double mutant produces a reduced number of papillae and haustorial encasements in response to Bgh, indicating an additive role of the exocyst in SYP121-coordinated non-host resistance. In summary, we report cooperation between the plant exocyst and a SNARE protein in penetration resistance against non-adapted fungal pathogens.
在非适应性禾本科布氏白粉菌(Bgh)的反应中,拟南芥叶表皮细胞沉积细胞壁增强物,称为乳突或密封真菌吸器在囊中,这两者都涉及到强烈的胞吐作用。已经发现植物 SNARE 蛋白 SYP121/PEN1 对于乳突的及时形成至关重要,并且囊泡连接复合物外泌体亚基 EXO70B2 已被发现有助于其形态。在这里,我们确定了 EXO70B2 包含的外泌体复合物在乳突膜域中的特定作用,这些膜域对于 callose 沉积和 GFP-SYP121 递送到焦点攻击部位很重要,以及其对囊封形成的贡献。mRuby2-EXO70B2 与外泌体核心亚基 SEC6 和 GFP-SYP121 在乳突的膜域中共同定位,并且 EXO70B2 和 SYP121 蛋白具有直接相互作用的能力。exo70B2/syp121 双突变体在响应 Bgh 时产生较少的乳突和吸器囊封,表明外泌体在 SYP121 协调的非寄主抗性中具有附加作用。总之,我们报告了植物外泌体与 SNARE 蛋白在抗非适应性真菌病原体穿透抗性中的合作。