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The OsGSK2 Kinase Integrates Brassinosteroid and Jasmonic Acid Signaling by Interacting with OsJAZ4

文献类型: 外文期刊

作者: He, Yuqing 1 ; Hong, Gaojie 1 ; Zhang, Hehong 2 ; Tan, Xiaoxiang 2 ; Li, Lulu 2 ; Kong, Yaze 1 ; Sang, Tian 3 ; Xie, Kail 1 ;

作者机构: 1.Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, State Key Lab Managing Biot & Chem Threats Qual &, Key Lab Biotechnol Plant Protect,Minist Agr & Zhe, Hangzhou 310021, Peoples R China

2.Ningbo Univ, Inst Plant Virol, Key Lab Biotechnol Plant Protect,Minist Agr & Zhe, State Key Lab Managing Biot & Chem Threats Qual &, Ningbo 315211, Peoples R China

3.Chinese Acad Sci, Shanghai Ctr Plant Stress Biol, CAS Ctr Excellence Mol Plant Sci, Shanghai 200032, Peoples R China

4.Chinese Acad Agr Sci, Inst Crop Sci, Beijing 100081, Peoples R China

5.Chinese Acad Sci, Inst Genet & Dev Biol, Beijing 100101, Peoples R China

期刊名称:PLANT CELL ( 影响因子:11.277; 五年影响因子:12.061 )

ISSN: 1040-4651

年卷期: 2020 年 32 卷 9 期

页码:

收录情况: SCI

摘要: The crosstalk between brassinosteroid (BR) and jasmonic acid (JA) signaling is crucial for plant growth and defense responses. However, the detailed interplay between BRs and JA remains obscure. Here, we found that the rice (Oryza sativa) Glycogen synthase kinase3 (GSK3)-like kinase OsGSK2, a conserved kinase serving as a key suppressor of BR signaling, enhanced antiviral defense and the JA response. We identified a member of the JASMONATE ZIM-domain (JAZ) family, OsJAZ4, as a OsGSK2 substrate and confirmed that OsGSK2 interacted with and phosphorylated OsJAZ4. We demonstrated that OsGSK2 disrupted the OsJAZ4-OsNINJA complex and OsJAZ4-OsJAZ11 dimerization by competitively binding to the ZIM domain, perhaps helping to facilitate the degradation of OsJAZ4 via the 26S proteasome pathway. We also showed that OsJAZ4 negatively modulated JA signaling and antiviral defense and that the BR pathway was involved in modulating the stability of OsJAZ4 protein in anOsCORONATINE INSENSITIVE1-dependent manner. Collectively, these results suggest that OsGSK2 enhances plant antiviral defenses by activating JA signaling as it directly interacts with, phosphorylates, and destabilizes OsJAZ4. Thus, our findings provide a clear link between BR and JA signaling. OsGSK2 directly interacts with and destabilizes OsJAZ4 to activate JA-mediated defense signaling.

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