Endocytosis is a crucial cellular process in eukaryotic cells which involves 
clathrin and/or adaptor proteins, lipid kinases, phosphatases and the actin 
cytoskeleton. Verprolin proteins, such as Vrp1 in Saccharomyces cerevisiae, are 
conserved family proteins that regulate actin binding and endocytosis. Here, we 
identified and characterized MoVrp1 as the yeast Vrp1 homolog in Magnaporthe 
oryzae. Deletion of the MoVRP1 gene resulted in defects in vegetative growth, 
asexual development, and infection of the host plant. The ∆Movrp1 mutants also 
exhibited decreased extracellular peroxidase and laccase activities and showed 
defects in colony pigmentation, hyphal surface hydrophobicity, cell wall 
integrity, autophagy, endocytosis, and secretion of avirulent effector. Our 
studies provided new evidences that MoVrp1 involved in actin cytoskeleton is 
important for growth, morphogenesis, cellular trafficking, and fungal 
pathogenesis.