부산대학교 도서관

GTP-binding protein (G-protein) and regulator of G-protein signaling (RGS) mediated signal transduction are critical in the growth and virulence of the rice blast pathogen Magnaporthe oryzae. We have previously reported that there are eight RGS and RGS-like proteins named MoRgs1 to MoRgs8 playing distinct and shared regulatory functions in M. oryzae and that MoRgs1 has a more prominent role compared to others in the fungus. To further explore the unique regulatory mechanism of MoRgs1, we screened a M. oryzae cDNA library for genes encoding MoRgs1-interacting proteins and identified MoCkb2, one of the two regulatory subunits of the casein kinase (CK) 2 MoCk2. We found that MoCkb2 and the sole catalytic subunit MoCka1 are required for the phosphorylation of MoRgs1 at the plasma membrane (PM) and late endosome (LE). We further found that an endoplasmic reticulum (ER) membrane protein complex (EMC) subunit, MoEmc2, modulates the phosphorylation of MoRgs1 by MoCk2. Interestingly, this phosphorylation is also essential for the GTPase-activating protein (GAP) function of MoRgs1. The balance among MoRgs1, MoCk2, and MoEmc2 ensures normal operation of the G-protein MoMagA-cAMP signaling required for appressorium formation and pathogenicity of the fungus. This has been the first report that an EMC subunit is directly linked to G-protein signaling through modulation of an RGS-casein kinase interaction. Author summary: G-proteins play a significant role in signal perception and transduction during pathogen and host interactions. In the rice blast fungus M. oryzae, previous studies demonstrated that G-protein/cAMP signaling are important for appressorium formation and pathogenicity. One of the eight regulator of G-protein signaling (RGS) and RGS-like proteins, MoRgs1, targets G-protein MoMagA to regulate cAMP levels and growth and virulence of the fungus; however, how MoRgs1 exhibits this function and its own regulation indifferent from other RGS and RGS-like proteins are not clear. We here demonstrated that MoRgs1 is subject to regulation by the casein kinase 2 MoCk2 through protein phosphorylation, and this regulation is also essential for the GTPase-activating protein (GAP) function of MoRgs1. We also showed that the endoplasmic reticulum (ER) membrane complex (EMC) subunit MoEmc2 modulates MoCk2-mediated MoRgs1 phosphorylation. Balanced interactions among MoRgs1, MoEmc2, and MoCk2 ensure normal appressorium formation and pathogenicity of M. oryzae. [ABSTRACT FROM AUTHOR]