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MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae

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...

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Autores principales: Qian, Bin, Su, Xiaotong, Ye, Ziyuan, Liu, Xinyu, Liu, Muxing, Zhang, Haifeng, Wang, Ping, Zhang, Zhengguang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10101639/
https://www.ncbi.nlm.nih.gov/pubmed/37011084
http://dx.doi.org/10.1371/journal.ppat.1011251
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author Qian, Bin
Su, Xiaotong
Ye, Ziyuan
Liu, Xinyu
Liu, Muxing
Zhang, Haifeng
Wang, Ping
Zhang, Zhengguang
author_facet Qian, Bin
Su, Xiaotong
Ye, Ziyuan
Liu, Xinyu
Liu, Muxing
Zhang, Haifeng
Wang, Ping
Zhang, Zhengguang
author_sort Qian, Bin
collection PubMed
description 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.
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spelling pubmed-101016392023-04-14 MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae Qian, Bin Su, Xiaotong Ye, Ziyuan Liu, Xinyu Liu, Muxing Zhang, Haifeng Wang, Ping Zhang, Zhengguang PLoS Pathog Research Article 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. Public Library of Science 2023-04-03 /pmc/articles/PMC10101639/ /pubmed/37011084 http://dx.doi.org/10.1371/journal.ppat.1011251 Text en © 2023 Qian et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Qian, Bin
Su, Xiaotong
Ye, Ziyuan
Liu, Xinyu
Liu, Muxing
Zhang, Haifeng
Wang, Ping
Zhang, Zhengguang
MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae
title MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae
title_full MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae
title_fullStr MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae
title_full_unstemmed MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae
title_short MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae
title_sort moerv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of magnaporthe oryzae
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10101639/
https://www.ncbi.nlm.nih.gov/pubmed/37011084
http://dx.doi.org/10.1371/journal.ppat.1011251
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