8.A.61.1.11
Complex protein II (COPII), Erv14, of 138 aas and 3 TMSs.  MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae (Qian et al. 2023). Magnaporthe oryzae causes rice blasts. During infection, M. oryzae utilizes several transmembrane receptor proteins that sense cell surface cues to induce highly specialized infectious structures called appressoria. Qian et al. 2023 showed that disrupting the coat protein complex II (COPII) cargo protein MoErv14 severely affected appressorium formation and pathogenicity as the ΔMoerv14 mutant is defective not only in cAMP production but also in the phosphorylation of the mitogen-activated protein kinase (MAPK) MoPmk1. Either externally supplementing cAMP or maintaining MoPmk1 phosphorylation suppressed the observed defects in the ΔMoerv14 strain. MoErv14 regulates the transport of MoPth11, a membrane receptor functioning upstream of G-protein/cAMP signaling, and MoWish and MoSho1 function upstream of the Pmk1-MAPK pathway. Thus, the mechanism by which Erv14 functions in regulating the transport of receptors involved in appressorium formation and virulence of the blast fungus was revealed (Qian et al. 2023).