SUMOylation controls peptide processing to generate damage-associated molecular patterns in Arabidopsis.

Autor:	Zhang C; Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou 510631, China., Wu Y; Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou 510631, China., Liu J; State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, China., Song B; Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou 510631, China., Yu Z; Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou 510631, China., Li JF; State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources, MOE Key Laboratory of Gene Function and Regulation, School of Life Sciences, Sun Yat-Sen University, Guangzhou 510275, China. Electronic address: lijfeng3@mail.sysu.edu.cn., Yang C; Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou 510631, China. Electronic address: yangchw@scnu.edu.cn., Lai J; Guangdong Provincial Key Laboratory of Biotechnology for Plant Development, School of Life Science, South China Normal University, Guangzhou 510631, China. Electronic address: 20141062@m.scnu.edu.cn.
Jazyk:	angličtina
Zdroj:	Developmental cell [Dev Cell] 2024 Nov 29. Date of Electronic Publication: 2024 Nov 29.
DOI:	10.1016/j.devcel.2024.11.010
Abstrakt:	Upon injury, both mammalian and plant cells activate a survival mechanism by sensing endogenous damage-associated molecular patterns (DAMPs). Plant elicitor peptides (Peps), a representative DAMP, are released from their precursors (PROPEPs; Precursors of Peps) through cleavage by metacaspases (MCs), but the control of Pep generation remains unclear. Here, we discovered that several PROPEPs in Arabidopsis thaliana are substrates for SUMOylation and that Ca 2+ upregulates PROPEP1 SUMOylation, facilitated by the SUMO E3 ligase SAP and MIZ1 domain-containing ligase1 (SIZ1). Mutations at the SUMOylation site on PROPEP1, or at the SUMO-interacting motifs (SIMs) on its protease MC4, reduced the PROPEP1-MC4 association and PROPEP1 cleavage. Overexpression of the wild-type form, but not the SUMOylation-defective variant of PROPEP1, enhanced plant tolerance to cell wall damage. Consistently, SIZ1 contributes to PROPEP1 processing and cell wall damage responses. These findings support the idea that SUMOylation promotes PROPEP1 cleavage via MC4 and provide insights into how DAMP generation is controlled in eukaryotic cells. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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