Document Type
Article
Publication Date
4-3-2023
Publication Title
PLoS Pathogens
Abstract
Magnaporthe oryzae causes rice blasts posing serious threats to food security worldwide. During infection, M. oryzae utilizes several transmembrane receptor proteins that sense cell surface cues to induce highly specialized infectious structures called appressoria. However, little is known about the mechanisms of intracellular receptor tracking and their function. Here, we described that disrupting the coat protein complex II (COPII) cargo protein MoErv14 severely affects 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. Studies also showed that either externally supplementing cAMP or maintaining MoPmk1 phosphorylation suppresses the observed defects in the ΔMoerv14 strain. Importantly, MoErv14 is found to regulate 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. In summary, our studies elucidate the mechanism by which the COPII protein MoErv14 plays an important function in regulating the transport of receptors involved in the appressorium formation and virulence of the blast fungus.
First Page
e1011251
PubMed ID
37011084
Volume
19
Issue
4
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Qian, Bin; Su, Xiaotong; Ye, Ziyuan; Liu, Xinyu; Liu, Muxing; Zhang, Haifeng; Wang, Ping; and Zhang, Zhengguang, "MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae" (2023). School of Graduate Studies Faculty Publications. 67.
https://digitalscholar.lsuhsc.edu/sogs_facpubs/67
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Cells Commons, Fungi Commons, Medical Microbiology Commons, Plants Commons