MoVast2 combined with MoVast1 regulates lipid homeostasis and autophagy in Magnaporthe oryzae
文献类型： 外文期刊
作者： Zhu, Xue-Ming 1 ; Li, Lin 1 ; Bao, Jian-Dong 1 ; Wang, Jiao-Yu 1 ; Liang, Shuang 1 ; Zhao, Li-Li 1 ; Huang, Chang-Li 1 ; Yan, Jiong-Yi 2 ; Cai, Ying-Ying 2 ; Wu, Xi-Yu 2 ; Dong, Bo 3 ; Liu, Xiao-Hong 2 ; Klionsky, Daniel J. 4 ; Lin, Fu-Cheng 1 ;
作者机构： 1.Zhejiang Acad Agr Sci, Inst Plant Protect & Microbiol, State Key Lab Managing Biot & Chem Treats Qual & S, Hangzhou, Zhejiang, Peoples R China
2.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol, Hangzhou, Zhejiang, Peoples R China
3.Univ Kentucky, Coll Med, Markey Canc Ctr, Lexington, KY USA
4.Univ Michigan, Life Sci Inst, Ann Arbor, MI USA
5.Univ Michigan, Dept Mol Cellular & Dev Biol, Ann Arbor, MI USA
关键词： Autophagy; lipid homeostasis; magnaporthe oryzae; regulation; TORC2
期刊名称：AUTOPHAGY （ 影响因子：13.3； 五年影响因子：14.5 ）
ISSN： 1554-8627
年卷期： 2023 年 19 卷 8 期
页码：
收录情况： SCI
摘要： Macroautophagy/autophagy is an evolutionarily conserved biological process among eukaryotes that degrades unwanted materials such as protein aggregates, damaged mitochondria and even viruses to maintain cell survival. Our previous studies have demonstrated that MoVast1 acts as an autophagy regulator regulating autophagy, membrane tension, and sterol homeostasis in rice blast fungus. However, the detailed regulatory relationships between autophagy and VASt domain proteins remain unsolved. Here, we identified another VASt domain-containing protein, MoVast2, and further uncovered the regulatory mechanism of MoVast2 in M. oryzae. MoVast2 interacted with MoVast1 and MoAtg8, and colocalized at the PAS and deletion of MoVAST2 results in inappropriate autophagy progress. Through TOR activity analysis, sterols and sphingolipid content detection, we found high sterol accumulation in the Delta Movast2 mutant, whereas this mutant showed low sphingolipids and low activity of both TORC1 and TORC2. In addition, MoVast2 colocalized with MoVast1. The localization of MoVast2 in the MoVAST1 deletion mutant was normal; however, deletion of MoVAST2 leads to mislocalization of MoVast1. Notably, the wide-target lipidomic analyses revealed significant changes in sterols and sphingolipids, the major PM components, in the Delta Movast2 mutant, which was involved in lipid metabolism and autophagic pathways. These findings confirmed that the functions of MoVast1 were regulated by MoVast2, revealing that MoVast2 combined with MoVast1 maintained lipid homeostasis and autophagy balance by regulating TOR activity in M. oryzae.
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