MoSey1 regulates the unfolded protein response, appressorium development, and pathogenicity of Magnaporthe oryzae

文献类型： 外文期刊

第一作者： Yang, Zifeng

作者： Yang, Zifeng;Li, Meiqin;Huang, Linwan;Chen, Xinru;Weng, Shuning;Jules, Biregeya;Felix, Abah;Zheng, Huakun;Chen, Xiaofeng;Zhang, Jun;Wang, Zonghua;Tang, Wei;Li, Meiqin;Chen, Xiaofeng;Wang, Zonghua;Cai, Yingying;Tang, Wei;Liang, Jingang

作者机构：

关键词： Endoplasmic reticulum; Magnaporthe oryzae; Pathogenicity; Protein secretion; MoSey1

期刊名称：PHYTOPATHOLOGY RESEARCH （ 影响因子：3.2； 五年影响因子：3.7 ）

ISSN： 2096-5362

年卷期： 2024 年 6 卷 1 期

页码：

收录情况： SCI

摘要： Endoplasmic reticulum (ER) is an enclosed three-dimensional eukaryotic membrane network composed of flattened sacs. Fusion of homologous membranes to the ER membrane is essential for the maintenance of this network structure. In yeast, ER membrane fusion is mediated by Sey1p, whose paralogues function distinctly in different species. In this study, we investigated the biological functions of MoSEY1 in the devastating rice blast fungus Magnaporthe oryzae by functional genomic approach. Compared to wild type, deletion of MoSEY1 considerably decreased the growth and conidia production of M. oryzae. Additionally, the absence of MoSEY1 delayed appressorium formation and invasive hyphae growth. The appressorium function was also impaired in Delta Mosey1 mutant. Subcellular localization analysis revealed that MoSey1 is localized at the ER. The Delta Mosey1 mutant showed augmented sensitivity to ER stress. Additionally, we found that MoSey1 regulated the unfolded protein response, autophagy, and protein secretion in M. oryzae. In conclusion, our study unveiled the involvement of MoSey1 in the development, pathogenesis, and ER functions in M. oryzae.

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