Receptor-like cytoplasmic kinases PBL34/35/36 are required for CLE peptide-mediated signaling to maintain SAM and RAM homeostasis in Arabidopsis

Receptor-like cytoplasmic kinases PBL34/35/36 are required for CLE peptide-mediated signaling to maintain SAM and RAM homeostasis in Arabidopsis
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拟南芥中 CLE 肽介导的信号传导需要类受体细胞质激酶 PBL34/35/36 来维持 SAM 和 RAM 稳态。

DOI:
10.1093/plcell/koab315
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发表时间:
2021
期刊:
影响因子:
11.6
通讯作者:
Jing Yi
Jing Yi
中科院分区:
生物学1区
文献类型:
--
作者:
Wenping Wang;Chong Hu;Xiaonan Li;Yafen Zhu;Liang Tao;Yanwei Cui;Dingqian Deng;Xiaoxuan Fan;Hong Zhang;Jia Li;Xiaoping Gou;Jing Yi

文献摘要

相似文献

芽顶端分生组织(SAM)和根顶端分生组织(RAM)的稳态由CLAVATA 3(CLV 3)/胚周围区域相关(CLE)肽信号传导紧密调节。然而,在CLV 3被CLV 1-CLV 3-不敏感激酶(CIK)受体复合物感知和CLE 25/26/45被几乎任何分生组织(BAM)-CIK受体复合物感知之后的细胞内信号传导组分是未知的。在这里,我们报告PBS 1-LIKE 34/35/36(PBL 34/35/36),受体样细胞质激酶的一个分支,需要CLV 3介导的信号在SAM和CLE 25/26/45介导的信号在RAM。生理测定表明,pbl 34 pbl 35 pbl 36的SAM和RAM分别对CLV 3和CLE 25/26/45处理具有抗性。遗传分析表明,pbl 34、pbl 35、pbl 36对clv 2和rpk 2的SAM缺陷有显著的加性效应,而对clv 1无显著的加性效应,对bam 3和cik 2无加性效应。进一步的生化分析显示,PBL 34/35/36与CLV 1、BAM 1/3和CIK相互作用,并被CLV 1和BAM 1磷酸化。所有这些结果表明,PBL 34/35/36作用于CLV 1和BAM 1/3的下游,分别介导CLV 3和CLE 25/26/45信号维持SAM和RAM稳态。我们的发现揭示了CLE信号在被细胞表面受体复合物感知后如何在细胞内传递。
Shoot apical meristem (SAM) and root apical meristem (RAM) homeostasis is tightly regulated by CLAVATA3 (CLV3)/EMBRYO SURROUNDING REGION-related (CLE) peptide signaling. However, the intracellular signaling components after CLV3 is perceived by the CLV1–CLV3-INSENSITIVE KINASE (CIK) receptor complex and CLE25/26/45 are sensed by the BARELY ANY MERISTEM (BAM)–CIK receptor complex are unknown. Here, we report that PBS1-LIKE34/35/36 (PBL34/35/36), a clade of receptor-like cytoplasmic kinases, are required for both CLV3-mediated signaling in the SAM and CLE25/26/45-mediated signaling in the RAM. Physiological assays showed that the SAM and RAM ofpbl34 pbl35 pbl36were resistant to CLV3 and CLE25/26/45 treatment, respectively. Genetic analyses indicated thatpbl34 pbl35 pbl36greatly enhanced the SAM defects ofclv2andrpk2but notclv1, and did not show additive effects withbam3andcik2in the RAM. Further biochemical assays revealed that PBL34/35/36 interacted with CLV1, BAM1/3, and CIKs, and were phosphorylated by CLV1 and BAM1. All these results suggest that PBL34/35/36 act downstream of CLV1 and BAM1/3 to mediate the CLV3 and CLE25/26/45 signals in maintaining SAM and RAM homeostasis, respectively. Our findings shed light on how CLE signals are transmitted intracellularly after being perceived by cell surface receptor complexes.