Smith John M, Salamango Daniel J, Leslie Michelle E, Collins Carina A, Heese Antje
Division of Biochemistry, Interdisciplinary Plant Group , University of Missouri, Columbia, Missouri 65211.
Plant Physiol. 2014 Jan;164(1):440-54. doi: 10.1104/pp.113.229179. Epub 2013 Nov 12.
FLAGELLIN-SENSING2 (FLS2) is the plant cell surface receptor that perceives bacterial flagellin or flg22 peptide, initiates flg22-signaling responses, and contributes to bacterial growth restriction. Flg22 elicitation also leads to ligand-induced endocytosis and degradation of FLS2 within 1 h. Why plant cells remove this receptor precisely at the time during which its function is required remains mainly unknown. Here, we assessed in planta flg22-signaling competency in the context of ligand-induced degradation of endogenous FLS2 and chemical interference known to impede flg22-dependent internalization of FLS2 into endocytic vesicles. Within 1 h after an initial flg22 treatment, Arabidopsis (Arabidopsis thaliana) leaf tissue was unable to reelicit flg22 signaling in a ligand-, time-, and dose-dependent manner. These results indicate that flg22-induced degradation of endogenous FLS2 may serve to desensitize cells to the same stimulus (homologous desensitization), likely to prevent continuous signal output upon repetitive flg22 stimulation. In addition to impeding ligand-induced FLS2 degradation, pretreatment with the vesicular trafficking inhibitors Wortmannin or Tyrphostin A23 impaired flg22-elicited reactive oxygen species production that was partially independent of BRASSINOSTEROID INSENSITIVE1-ASSOCIATED KINASE1. Interestingly, these inhibitors did not affect flg22-induced mitogen-activated protein kinase phosphorylation, indicating the ability to utilize vesicular trafficking inhibitors to target different flg22-signaling responses. For Tyrphostin A23, reduced flg22-induced reactive oxygen species could be separated from the defect in FLS2 degradation. At later times (>2 h) after the initial flg22 elicitation, recovery of FLS2 protein levels positively correlated with resensitization to flg22, indicating that flg22-induced new synthesis of FLS2 may prepare cells for a new round of monitoring the environment for flg22.
鞭毛蛋白感应蛋白2(FLS2)是植物细胞表面受体,可感知细菌鞭毛蛋白或flg22肽,启动flg22信号应答,并有助于限制细菌生长。flg22诱导还会导致配体诱导的内吞作用以及FLS2在1小时内降解。植物细胞为何恰好在需要该受体功能时精确地去除它,这一点仍主要未知。在这里,我们在内源FLS2配体诱导降解以及已知会阻碍FLS2依赖flg22进入内吞小泡的化学干扰的背景下,评估了植物体内flg22信号传导能力。在初次flg22处理后1小时内,拟南芥(Arabidopsis thaliana)叶片组织无法以配体、时间和剂量依赖的方式再次引发flg22信号。这些结果表明,flg22诱导的内源FLS2降解可能使细胞对相同刺激脱敏(同源脱敏),可能是为了防止在重复flg22刺激时持续输出信号。除了阻碍配体诱导的FLS2降解外,用囊泡运输抑制剂渥曼青霉素或酪氨酸磷酸化抑制剂A23预处理会损害flg22诱导的活性氧产生,这部分独立于油菜素内酯不敏感1相关激酶1。有趣的是,这些抑制剂不影响flg22诱导的丝裂原活化蛋白激酶磷酸化,表明能够利用囊泡运输抑制剂靶向不同的flg22信号应答。对于酪氨酸磷酸化抑制剂A23,flg22诱导的活性氧减少可与FLS2降解缺陷区分开来。在初次flg22诱导后的后期(>2小时),FLS2蛋白水平的恢复与对flg重新敏感化呈正相关,表明flg22诱导的FLS2新合成可能使细胞为新一轮监测flg22环境做好准备。