Environmental Microbiology · 2017 · 22 citations · 43 references
Life SciencesBiologyMolecular BiologyEndocytosisMycologyPlant-microbe InteractionsEndomembrane SystemEndosomal TraffickingFungal Cell BiologyFungal PathogenesisPlant-pathogen InteractionsProtein SortingBar DomainsEndosomal FusionEndosome FusionFungal MorphogenesisRetromer ComplexRetromer-mediated SortingSorting Nexin ProteinsSorting Nexins
Vps17 is a sorting nexin (SNX) and a component of the retromer, a protein complex mediating retrograde vesicle transport between endosomes and the trans-Golgi network. However, its role in the development and pathogenicity of filamentous fungi such as the rice blast fungus (Magnaporthe oryzae) remains unclear. We investigate the functional relationship between the SNX and the cargo-selective complex (CSC) of the fungal retromer by genetic analysis, live cell imaging and immunological assay. Our data show that the MoVps17 null mutation causes defects in growth, development and pathogenicity in M. oryzae. MoVps17 is localized to endosomes depending on the activity of phosphatidylinositol 3-kinase (PI3K), a key enzyme for fungal development and infection. Both PX and BAR domains of MoVps17 are essential for its endosomal localization and function. Furthermore, our yeast two-hybrid assays show that MoVps17 and MoVps5 can interact. Lastly, live cell imaging suggests that MoVps17 can regulate early endosome fusion and budding as well as endocytosis. Taken together, our results suggest that MoVps17 specifically functions as a retromer component with CSC and also plays a distinct role in the regulation of endosome dynamics during fungal development and plant infection.
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