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Abstract：
Fsr1, a homologue of mammalian striatin, containing multiple protein-binding domains and a coiled-coil (CC) domain, is critical for Fusarium verticillioides virulence. In mammals, striatin interacts with multiple proteins to form a STRIPAK (striatin-interacting phosphatase and kinase) complex that regulates a variety of developmental processes and cellular mechanisms. In this study, we identified the homologue of a key mammalian STRIPAK component STRIP1/2 (striatin-interacting proteins 1 and 2) in F. verticillioides, FvStp1, which interacts with Fsr1 in vivo. Gene deletion analysis indicates that FvStp1 is critical for F. verticillioides stalk rot virulence. In addition, we identified three proteins, designated FvCyp1, FvScp1 and FvSel1, which interact with the Fsr1 CC domain via a yeast two-hybrid screen. Importantly, FvCyp1, FvScp1 and FvSel1 co-localize to endomembrane structures, each having a preferred localization in the cell, and they are all required for F. verticillioides stalk rot virulence. Moreover, these proteins are necessary for the correct localization of Fsr1 to the endoplasmic reticulum (ER) and nuclear envelope. Thus, we identified several novel components in the STRIPAK complex that regulates F. verticillioides virulence, and propose that the correct organization and localization of Fsr1 are critical for STRIPAK complex function.
摘要：
Fsr1，哺乳动物纹状体素的同源物，含有多个蛋白质结合结构域和卷曲螺旋（CC）结构域，对轮状镰刀菌毒力至关重要。在哺乳动物中,纹状体蛋白与多种蛋白质相互作用，形成STRIPAK（纹状体蛋白相互作用的磷酸酶和激酶）复合物，该复合物调节多种发育过程和细胞机制。在这项研究中,我们鉴定了轮虫中关键哺乳动物STRIPAK组分STRIP1/2（纹状体蛋白相互作用蛋白1和2）的同源物，FvStp1，在体内与Fsr1相互作用。基因缺失分析表明，FvStp1对轮虫茎腐病毒力至关重要。此外,我们鉴定了三种蛋白质，命名为FvCyp1，FvScp1和FvSel1，它们通过酵母双杂交筛选与Fsr1CC结构域相互作用。重要的是,FvCyp1，FvScp1和FvSel1共同定位为内膜结构，每个在细胞中都有一个优选的定位，它们都是轮虫茎腐病毒力所必需的。此外，这些蛋白质对于Fsr1正确定位内质网（ER）和核膜是必需的。因此，我们在STRIPAK复合物中发现了几种新的成分，这些成分可以调节轮虫毒力，并提出Fsr1的正确组织和定位对于STRIPAK复杂功能至关重要。
