During host-pathogen interactions, pathogens employ endolysosomal trafficking to fine-tune host and environmental cues, facilitating disease progression. Inhibiting the functions of the endolysosomal network could be promising for the control of plant fungal diseases. Herein, we showed that inhibition of the endocytic dynamin FgVps1 by the phenothiazines chlorpromazine (CPZ) and prochlorperazine (PCZ) leads to endolysosomal dysfunction. Further analyses revealed that the phenothiazines directly bind the GTPase domain of FgVps1 to inhibit its activity. Moreover, our results showed that FgVps1 is recruited to the endosome by the Rab GTPases FgRab51 and FgRab7 to facilitate the release of retromer- and sorting nexin-coated vesicles, thereby ensuring the proper recycling of some cargos and promoting fungal development and pathogenicity. Direct treatment of the phytopathogensF. graminearum,Magnaporthe oryzaeandFusarium oxysporum f. sp. cubensewith CPZ and PCZ also impairs their growth, development and virulence. These results unveil the underlying mechanisms of endocytic dynamin actions and provide a potential strategy for broad-spectrum control of phytopathogenic fungi.