配体诱导的BIK1单泛素化调节植物免疫力
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配体诱导的BIK1单泛素化调节植物免疫力

作者: 美高梅赌城注册 时间: 2020-04-23 20:24 点击:

本期文章:《自然》:Online/在线发表

美国德州农工大学Libo Shan、Ping He等研究人员合作发现,配体诱导的BIK1单泛素化调节植物免疫力。相关论文于2020年4月22日在线发表在《自然》杂志上。

研究人员表示,模式识别受体(PRR)对微生物相关分子模式(MAMP)的识别触发了针对入侵病原菌的第一道诱导性防御。受体样细胞质激酶(RLCK)是与植物中多个PRR相关的调节因子。RLCK激活的机制尚不清楚。

 

研究人员发现,当检测到MAMP时,RLCK细菌诱导的激酶1(BIK1)在磷酸化后被单泛素化,然后从flagellin 受体FLS2(FLAGELLIN SENSING 2)-BAK1(BRASSINOSTEROID INSERTSITIVE 1-ASSOCIATED KINASE 1)复合物中释放,并动态转移到到内吞室。

 

拟南芥E3泛素连接酶RING-H2 RHA3A(FINGER A3A)和RHA3B介导BIK1的单泛素化,这对于BIK1从FLS2-BAK1复合体的后续释放和免疫信号的激活至关重要。配体诱导的BIK1的单泛素化和内吞体聚集显示出不同于PRR FLS2的时空动态。

 

这项研究揭示了蛋白磷酸化和泛素化对PRR–RLCK复合物活化的相互调节,并表明配体诱导的单泛素化有助于BIK1家族RLCK从PRR复合物中的释放和PRR信号的活化。

 

附:英文原文

 

Title: Ligand-induced monoubiquitination of BIK1 regulates plant immunity

Author: Xiyu Ma, Lucas A. N. Claus, Michelle E. Leslie, Kai Tao, Zhiping Wu, Jun Liu, Xiao Yu, Bo Li, Jinggeng Zhou, DanielV. Savatin, Junmin Peng, Brett M. Tyler, Antje Heese, Eugenia Russinova, Ping He, Libo Shan

Issue&Volume: 2020-04-22

Abstract: Recognition of microbe-associated molecular patterns (MAMPs) by pattern recognition receptors (PRRs) triggers the first line of inducible defence against invading pathogens1,2,3. Receptor-like cytoplasmic kinases (RLCKs) are convergent regulators that associate with multiple PRRs in plants4. 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.

DOI: 10.1038/s41586-020-2210-3

Source: https://www.nature.com/articles/s41586-020-2210-3

期刊信息

Nature:《自然》,创刊于1869年。隶属于施普林格·自然出版集团,最新IF:43.07
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