The Paxillin MoPax1 Activates Mitogen-Activated Protein (MAP) Kinase Signaling Pathways and Autophagy through MAP Kinase Activator MoMka1 during Appressorium-Mediated Plant Infection by the Rice Blast Fungus Magnaporthe oryzae.

Paxillin is a focal adhesion-associated protein that functions as an adaptor to recruit diverse cytoskeleton and signaling molecules into a complex and plays a crucial role in several signaling pathways in mammal cells. However, paxillin-mediated signal pathways are largely unknown in phytopathogenic fungi. Previously, Pax1 of Magnaporthe oryzae (MoPax1), a paxillin-like protein, has been identified as a crucial pathogenicity determinant. Here, we report the identification of a mitogen-activated protein (MAP) kinase (MAPK) activator, Mka1 of M. oryzae (MoMka1), that physically interacts with MoPax1. Targeted gene deletion of resulted in pleiotropic defects in aerial hyphal growth, conidiation, appressorium formation, and pathogenicity in M. oryzae. MoMka1 interacts with Mst50, an adaptor protein of the Mst11-Mst7-Pmk1 and Mck1-Mkk2-Mps1 cascades. Moreover, the phosphorylation levels of both Pmk1 and Mps1 in aerial hyphae of the mutant were significantly reduced, indicating that MoMka1 acts upstream from the MAPK pathways. Interestingly, we found that MoMka1 interacts with MoAtg6 and MoAtg13. Deletion of led to impaired MoAtg13 phosphorylation and enhanced autophagic flux under nutrient-rich conditions, indicating that MoMka1 is required for regulation of autophagy in M. oryzae. Taken together, the paxillin MoPax1 may activate MAP kinase signaling pathways and autophagy through MAP kinase activator MoMka1 and play important roles during appressorium-mediated plant infection by the rice blast fungus. Paxillin, as an adaptor recruiting diverse cytoskeleton and signaling molecules into a complex, plays a crucial role in several signaling pathways in mammal cells. However, paxillin-mediated signal pathways are largely unknown in phytopathogenic fungi. Here, we identified that MoMka1 physically interacts with MoPax1. Furthermore, MoMka1 acts upstream from the MAPK pathways through interacting with Mst50, a key protein of the Mst11-Mst7-Pmk1 and Mck1-Mkk2-Mps1 cascades. Meanwhile, MoMka1 interacts with both MoAtg6 and MoAtg13 and controls autophagy initiation by influencing the phosphorylation level of MoAtg13. In summary, we describe a model in which MoPax1 activates MAP kinase signaling pathways and autophagy through MoMka1 during appressorium-mediated plant infection by M. oryzae.