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配体诱导 BIk1 的单泛素化调节植物免疫。

Ligand-induced monoubiquitination of BIK1 regulates plant immunity.

机构信息

Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.

Institute for Plant Genomics and Biotechnology, Texas A&M University, College Station, TX, USA.

出版信息

Nature. 2020 May;581(7807):199-203. doi: 10.1038/s41586-020-2210-3. Epub 2020 Apr 22.

DOI:10.1038/s41586-020-2210-3
PMID:32404997
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7233372/
Abstract

Recognition of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) triggers the first line of inducible defence against invading pathogens. Receptor-like cytoplasmic kinases (RLCKs) are convergent regulators that associate with multiple PRRs in plants. The mechanisms that underlie the activation of RLCKs are unclear. Here we show that when MAMPs are detected, the RLCK BOTRYTIS-INDUCED KINASE 1 (BIK1) is monoubiquitinated following phosphorylation, then released from the flagellin receptor FLAGELLIN SENSING 2 (FLS2)-BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1 (BAK1) complex, and internalized dynamically into endocytic compartments. The Arabidopsis E3 ubiquitin ligases RING-H2 FINGER A3A (RHA3A) and RHA3B mediate the monoubiquitination of BIK1, which is essential for the subsequent release of BIK1 from the FLS2-BAK1 complex and activation of immune signalling. Ligand-induced monoubiquitination and endosomal puncta of BIK1 exhibit spatial and temporal dynamics that are distinct from those of the PRR FLS2. Our study reveals the intertwined regulation of PRR-RLCK complex activation by protein phosphorylation and ubiquitination, and shows that ligand-induced monoubiquitination contributes to the release of BIK1 family RLCKs from the PRR complex and activation of PRR signalling.

摘要

模式识别受体（PRRs）识别微生物相关分子模式（MAMPs），触发了针对入侵病原体的第一道诱导防御。类受体细胞质激酶（RLCKs）是植物中与多种 PRR 相关的汇聚调节剂。RLCK 激活的机制尚不清楚。在这里，我们表明，当检测到 MAMPs 时，RLCK BOTRYTIS-INDUCED KINASE 1（BIK1）在磷酸化后被单泛素化，然后从鞭毛受体 FLAGELLIN SENSING 2（FLS2）-BRASSINOSTEROID INSENSITIVE 1-ASSOCIATED KINASE 1（BAK1）复合物中释放出来，并动态内化到内吞体腔室中。拟南芥 E3 泛素连接酶 RING-H2 FINGER A3A（RHA3A）和 RHA3B 介导 BIK1 的单泛素化，这对于 BIK1 随后从 FLS2-BAK1 复合物中释放和免疫信号的激活是必不可少的。配体诱导的 BIK1 单泛素化和内体斑点显示出与 PRR FLS2 不同的时空动态。我们的研究揭示了蛋白磷酸化和泛素化对 PRR-RLCK 复合物激活的交织调控，并表明配体诱导的单泛素化有助于 BIK1 家族 RLCKs 从 PRR 复合物中释放并激活 PRR 信号。

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