A new plant SUMO ligase, MPEL1, synergizes with MAPK16 to regulate resistance against Fusarium pathogens

SUMOylation is critical for plant growth and defense, and the specific substrate recognition mediated by SUMO ligases dictates the biological processes in which SUMOylation functions. However, only four SUMO ligases involved in SUMOylation have been reported in plants. Here, we report MPEL1 as a new SUMO ligase in maize, which paradoxically exhibits SUMO ligase activity despite its sequence homology to SUMO-targeted ubiquitin ligases (STUbL). MPEL1 stabilizes the plant-specific mitogen-activated protein kinase 16 (MAPK16) via SUMOylation at Lys526 within C-terminal domain (CTD). MAPK16 directly binds to JAZ20 via its C-terminal domain and phosphorylates JAZ20 at Thr12/Ser13 residues, thereby triggering its proteasomal degradation and activating broad-spectrum resistance against two Fusarium pathogens. These pathogens cause devastating maize ear rot and stalk rot, leading to severe yield losses and serious food safety concerns worldwide. Notably, MAPK16 overexpression and JAZ20 knockout enhance disease resistance without yield penalty, highlighting their potential for crop improvement. These findings expand the plant SUMO ligase family and provide targets for breeding Fusarium-resistant crops.

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Publication Details

Journal
The EMBO Journal
Published
2026-05-18
DOI
https://doi.org/10.1038/s44318-026-00811-2
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
0.00

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article

A new plant SUMO ligase, MPEL1, synergizes with MAPK16 to regulate resistance against Fusarium pathogens

Haicheng Liao, Yunbi Xu, Yanli Lu, Xuanjun Feng et al.
The EMBO Journal
Ubiquitin and proteasome pathways
article

A new plant SUMO ligase, MPEL1, synergizes with MAPK16 to regulate resistance against Fusarium pathogens

Haicheng Liao, Yunbi Xu, Yanli Lu, Xuanjun Feng, Huarui Guan, Weixiao Zhang, Guangchao Sun, Xuemei Zhang, Yuting Chen, Huihui Xiao, Wang Wenming, Mengling Li, Yinzhi Li, Yaxi Liu, Haolan Yang, Xin Mao, Yuelin Zhang, Li Jia, Zhaoyu Zhang, Yizhen She, Na Wu, Muyan Liu, Shuang Cha, Hao Xiong
article en

Abstract

SUMOylation is critical for plant growth and defense, and the specific substrate recognition mediated by SUMO ligases dictates the biological processes in which SUMOylation functions. However, only four SUMO ligases involved in SUMOylation have been reported in plants. Here, we report MPEL1 as a new SUMO ligase in maize, which paradoxically exhibits SUMO ligase activity despite its sequence homology to SUMO-targeted ubiquitin ligases (STUbL). MPEL1 stabilizes the plant-specific mitogen-activated protein kinase 16 (MAPK16) via SUMOylation at Lys526 within C-terminal domain (CTD). MAPK16 directly binds to JAZ20 via its C-terminal domain and phosphorylates JAZ20 at Thr12/Ser13 residues, thereby triggering its proteasomal degradation and activating broad-spectrum resistance against two Fusarium pathogens. These pathogens cause devastating maize ear rot and stalk rot, leading to severe yield losses and serious food safety concerns worldwide. Notably, MAPK16 overexpression and JAZ20 knockout enhance disease resistance without yield penalty, highlighting their potential for crop improvement. These findings expand the plant SUMO ligase family and provide targets for breeding Fusarium-resistant crops.

The EMBO Journal
Peking University (CN), Sichuan University (CN), Sichuan Agricultural University (CN)
National Natural Science Foundation of China, Natural Science Foundation of Sichuan Province, National Key Research and Development Program of China
Zero hunger
Openalex Percentile: Top 8%
Ubiquitin and proteasome pathways
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