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A VASt-domain protein regulates autophagy, membrane tension, and sterol homeostasis in rice blast fungus

文献类型： 外文期刊

作者： Zhu, Xue-Ming 1 ; Li, Lin 1 ; Cai, Ying-Ying 1 ; Wu, Xi-Yu 1 ; Shi, Huan-Bin 1 ; Liang, Shuang 1 ; Qu, Ying-Min 1 ; Naqvi 1 ;

作者机构： 1.Zhejiang Univ, Inst Biotechnol, St Ate Key Lab Managing Biot & Chem Treats Qual &, Hangzhou, Peoples R China

2.Zhejiang Acad Agr Sci, Inst Plant Protect & Microbiol, State Key Lab Managing Biot & Chem Treats Qual &, Hangzhou, Zhejiang, Peoples R China

3.Natl Univ Singapore, Dept Biol Sci, Temasek Life Sci Lab, Singapore, Singapore

4.SUNY Stony Brook, Dept Microbiol & Immunol, Stony Brook, NY 11794 USA

5.SUNY Stony Brook, Div Infect Dis, Stony Brook, NY 11794 USA

6.Vet Affairs Med Ctr, Northport, NY USA

7.Univ Kentucky, Coll Med, Markey Canc Ctr, Lexington, KY USA

关键词： Autophagy; membrane tension; motor; rice blast fungus; sterol homeostasis; vast-domain protein

期刊名称：AUTOPHAGY （ 影响因子：16.016； 五年影响因子：16.586 ）

ISSN： 1554-8627

年卷期：

页码：

收录情况： SCI

摘要： Sterols are a class of lipids critical for fundamental biological processes and membrane dynamics. These molecules are synthesized in the endoplasmic reticulum (ER) and are transported bi-directionally between the ER and plasma membrane (PM). However, the trafficking mechanism of sterols and their relationship with macroautophagy/autophagy are still poorly understood in the rice blast fungus Magnaporthe oryzae. Here, we identified the VAD1 Analog of StAR-related lipid transfer (VASt) domain-containing protein MoVast1 via co-immunoprecipitation in M. oryzae. Loss of MoVAST1 resulted in conidial defects, impaired appressorium development, and reduced pathogenicity. The MoTor (target of rapamycin in M. oryzae) activity is inhibited because MoVast1 deletion leads to high levels of sterol accumulation in the PM. Site-directed mutagenesis showed that the 902 T site is essential for localization and function of MoVast1. Through filipin or Flipper-TR staining, autophagic flux detection, MoAtg8 lipidation, and drug sensitivity assays, we uncovered that MoVast1 acts as a novel autophagy inhibition factor that monitors tension in the PM by regulating the sterol content, which in turn modulates the activity of MoTor. Lipidomics and transcriptomics analyses further confirmed that MoVast1 is an important regulator of lipid metabolism and the autophagy pathway. Our results revealed and characterized a novel sterol transfer protein important for M. oryzae pathogenicity.

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