Distinctive phosphorylation pattern during mitotic exit network (MEN) regulation is important for the development and pathogenicity of Magnaporthe oryzae

Abstract

AbstractThe mitotic exit network (MEN) pathway is a vital kinase cascade regulating the timely and correct progress of cell division. In the rice blast fungus Magnaporthe oryzae, the MEN pathway, consisting of conserved protein kinases MoSep1 and MoMob1-MoDbf2, is important in the development and pathogenicity of the fungus. We found that deletion of MoSEP1 affects the phosphorylation of MoMob1, but not MoDbf2, in contrast to what was found in the buddy yeast Saccharomyces cerevisiae, and verified this finding by in vitro phosphorylation assay and mass spectrometry (MS) analysis. We also found that S43 residue is the critical phosphor-site of MoMob1 by MoSep1, and proved that MoSep1-dependent MoMob1 phosphorylation is essential for cell division during the development of M. oryzae. We further provided evidence demonstrating that MoSep1 phosphorylates MoMob1 to maintain the cell cycle during vegetative growth and infection. Taken together, our results revealed that the MEN pathway has both distinct and conservative functions in regulating the cell cycle during the development and pathogenesis of M. oryzae.