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The endosomal recycling of FgSnc1 by FgSnx41–FgSnx4 heterodimer is essential for polarized growth and pathogenicity in Fusarium graminearum
Author(s) -
Zheng Wenhui,
Lin Yahong,
Fang Wenqin,
Zhao Xu,
Lou Yi,
Wang Guanghui,
Zheng Huawei,
Liang Qifu,
Abubakar Yakubu Saddeeq,
Olsson Stefan,
Zhou Jie,
Wang Zonghua
Publication year - 2018
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/nph.15178
Subject(s) - endosome , microbiology and biotechnology , biology , rab , vacuole , vacuolar protein sorting , escrt , sorting nexin , tip growth , retromer , transport protein , intracellular , exocyst , small gtpase , cytoplasm , gtpase , vesicle , genetics , membrane , botany , signal transduction , pollen , pollination , pollen tube
Summary Endosomal sorting machineries regulate the transport of their cargoes among intracellular compartments. However, the molecular nature of such intracellular trafficking processes in pathogenic fungal development and pathogenicity remains unclear. Here, we dissect the roles and molecular mechanisms of two sorting nexin proteins and their cargoes in endosomal recycling in Fusarium graminearum using high‐resolution microscopy and high‐throughput co‐immunoprecipitation strategies. We show that the sorting nexins, FgSnx41 and FgSnx4, interact with each other and assemble into a functionally interdependent heterodimer through their respective BAR domains. Further analyses demonstrate that the dimer localizes to the early endosomal membrane and coordinates endosomal sorting. The small GTP ase FgRab5 regulates the correct localization of FgSnx41–FgSnx4 and is consequently required for its trafficking function. The protein FgSnc1 is a cargo of FgSnx41–FgSnx4 and regulates the fusion of secreted vesicles with the fungal growing apex and plasma membrane. In the absence of FgSnx41 or FgSnx4, FgSnc1 is mis‐sorted and degraded in the vacuole, and null deletion of either component causes defects in the fungal polarized growth and virulence. Overall, for the first time, our results reveal the mechanism of FgSnc1 endosomal recycling by FgSnx41–FgSnx4 heterodimer which is essential for polarized growth and pathogenicity in F. graminearum .