A subunit of the HOPS endocytic tethering complex, FgVps41, is important for fungal development and plant infection in Fusarium graminearum
文献类型： 外文期刊
作者： Li, Bing 1 ; Dong, Xin 1 ; Li, Xinrui 1 ; Chen, Huaigu 3 ; Zhang, Haifeng 1 ; Zheng, Xiaobo 1 ; Zhang, Zhengguang 1 ;
作者机构： 1.Nanjing Agr Univ, Coll Plant Protect, Dept Plant Pathol, Nanjing 210095, Jiangsu, Peoples R China
2.Minist Educ, Key Lab Integrated Management Crop Dis & Pests, Nanjing 210095, Jiangsu, Peoples R China
3.Jiangsu Acad Agr Sci, Inst Plant Protect, Nanjing 210014, Jiangsu, Peoples R China
期刊名称：ENVIRONMENTAL MICROBIOLOGY （ 影响因子：5.491； 五年影响因子：6.438 ）
ISSN： 1462-2912
年卷期： 2018 年 20 卷 4 期
页码：
收录情况： SCI
摘要： The signals by which eukaryotic cells communicate with the environment are usually mediated by vesicle trafficking to be attenuated or terminated. However, vesicle trafficking-mediated signal transmission during interactions between pathogens and host plants is poorly understood. Here, we identified and characterized the vacuole sorting protein FgVps41, which is the yeast HOPS tethering complex subunit Vps41 homolog in Fusarium graminearum. Targeted gene deletion demonstrated that FgVps41 is important for vegetative growth, asexual/sexual development, conidial morphology, plant infection and deoxynivalenol production. Cellular localization and cytological examinations revealed that FgVps41 localizes to early/late endosomes and vacuole membrane, and is recruited to prevacuolar compartments and vacuole membrane by interacting with FgRab7 in F. graminearum. Furthermore, we found FgVps41 mediates vacuole membrane fusion and sorting of FgApeI, a cargo protein involving in the cytosol-to-vacuole targeting pathway. In addition, we found that FgVps41 interacts with FgYck3, a vacuolar type I casein kinase, which regulates vesicle fusion in the AP-3 pathway. Deletion of FgYck3 showed similar phenotypes to the Delta Fgvps41 mutant, and both FgRab7 and FgYck3 regulate the normal localization of FgVps41. Collectively, our results demonstrate that FgVps41 acts as a HOPS tethering complex subunit and is important for the development of infection-related morphogenesis in F. graminearum.
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