The ArfGAP protein MoGlo3 regulates the development and pathogenicity of Magnaporthe oryzae.

ABSTRACT: The ADP ribosylation factor (Arf) and the coat protein complex I (COPI) are involved in vesicle transport. Together with GTPase-activating proteins (ArfGAPs) and guanine exchange factors (ArfGEFs) that regulate the activity of Arf, they govern vesicle formation, COPI trafficking and the maintenance of the Golgi complex. In an ongoing effort to study the role of membrane trafficking in pathogenesis of the rice blast fungus Magnaporthe oryzae, we identified MoGlo3 as an ArfGAP protein that is homologous to Glo3p of the budding yeast Saccharomyces cerevisiae. As suspected, MoGlo3 partially complements the function of yeast Glo3p. Consistent with findings in S. cerevisiae, MoGlo3 is localized to the Golgi, and that the localization is dependent on the conserved BoCCS domain. We found that MoGl

SUBMITTER: Zhang S 

PROVIDER: S-EPMC5861720 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature