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Deubiquitinase Ubp3 regulates ribophagy and deubiquitinates Smo1 for appressorium-mediated infection by Magnaporthe oryzae

文献类型： 外文期刊

作者： Cai, Xuan 1 ; Xiang, Shikun 2 ; He, Wenhui 2 ; Tang, Mengxi 2 ; Zhang, Shimei 2 ; Chen, Deng 2 ; Zhang, Xinrong 2 ; Liu, Caiyun 1 ; Li, Guotian 2 ; Xing, Junjie 4 ; Li, Yunfeng 1 ; Chen, Xiao-Lin 2 ; Nie, Yanfang 1 ;

作者机构： 1.South China Agr Univ, Lab Physiol Plant Pathol, Guangzhou, Peoples R China

2.Huazhong Agr Univ, Coll Plant Sci & Technol, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China

3.Huazhong Agr Univ, Coll Plant Sci & Technol, Prov Key Lab Plant Pathol Hubei Prov, Wuhan 430070, Peoples R China

4.Hunan Hybrid Rice Res Ctr, State Key Lab Hybrid Rice, Changsha, Peoples R China

5.South China Agr Univ, Coll Mat & Energy, Guangzhou, Peoples R China

关键词： appressorium formation; deubiquitinating enzyme; Ras signalling; ribophagy; ubiquitination

期刊名称：MOLECULAR PLANT PATHOLOGY （ 影响因子：5.52； 五年影响因子：6.25 ）

ISSN： 1464-6722

年卷期： 2022 年 23 卷 6 期

页码：

收录情况： SCI

摘要： The Ubp family of deubiquitinating enzymes has been found to play important roles in plant-pathogenic fungi, but their regulatory mechanisms are still largely unknown. In this study, we revealed the regulatory mechanism of the deubiquitinating enzyme Ubp3 during the infection process of Magnaporthe oryzae. AUBP3 deletion mutant was severely defective in appressorium turgor accumulation, leading to the impairment of appressorial penetration. During appressorium formation, the mutant was also defective in glycogen and lipid metabolism. Interestingly, we found that nitrogen starvation and rapamycin treatment induced the ribophagy process in M. oryzae, which is closely dependent on Ubp3. In the increment ubp3 mutant, the ribosome proteins and rRNAs were not well degraded on nitrogen starvation and rapamycin treatment. We also found that Ubp3 interacted with the GTPase-activating protein Smo1 and regulated its de-ubiquitination. Ubp3-dependent de-ubiquitination of Smo1 may be required for Smo1 to coordinate Ras signalling. Taken together, our results showed at least two roles of Ubp3 in M. oryzae: it regulates the ribophagy process and it regulates de-ubiquitination of GTPase-activating protein Smo1 for appressorium-mediated infection.

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