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。
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
Nature:《自然》,创刊于1869年。隶属于施普林格·自然出版集团,最新IF:69.504
官方网址:http://www.nature.com/
投稿链接:http://www.nature.com/authors/submit_manuscript.html
本期文章:《自然》:Online/在线发表