MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae.
MoErv14 mediates the intracellular transport of cell membrane receptors to govern the appressorial formation and pathogenicity of Magnaporthe oryzae.
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DOI：
10.1371/journal.ppat.1011251
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发表时间：
2023-04
期刊：
影响因子：
6.7
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稻瘟病引起稻瘟病，对全球粮食安全构成严重威胁。在感染过程中，米霉利用几种跨膜受体蛋白来感知细胞表面信号，诱导称为附着胞的高度特化的感染结构。然而，人们对细胞内受体追踪的机制及其功能知之甚少。在这里，我们描述了破坏外壳蛋白复合物 II (COPII) 货物蛋白 MoErv14 会严重影响附着胞的形成和致病性，因为 ΔMoerv14 突变体不仅在 cAMP 产生方面存在缺陷，而且在丝裂原激活蛋白激酶 (MAPK) MoPmk1 的磷酸化方面也存在缺陷。研究还表明，外部补充 cAMP 或维持 MoPmk1 磷酸化可抑制 ΔMoerv14 菌株中观察到的缺陷。重要的是，MoErv14被发现可以调节MoPth11（一种在G蛋白/cAMP信号传导上游发挥作用的膜受体）的转运，而MoWish和MoSho1在Pmk1-MAPK通路上游发挥作用。总之，我们的研究阐明了 COPII 蛋白 MoErv14 在调节参与附着胞形成和瘟疫真菌毒力的受体运输中发挥重要功能的机制。在与水稻的致病相互作用过程中，稻瘟病菌感知细胞表面信号并形成一种高度特化的感染结构，称为附着胞，从而引发感染。研究表明，几种跨膜蛋白对于感知水稻宿主信号至关重要。然而，人们对这些跨膜蛋白如何在细胞内运输以影响附着胞形成和致病性知之甚少。在这项研究中，我们发现MoErv14对于稻瘟菌的生长和致病性很重要，并且MoErv14调节多种膜传感器的运输，包括MoPth11、MoWish和MoSho1，这些传感器在G蛋白/cAMP信号传导或Pmk1-MAPK通路的上游发挥作用。重要的是，我们发现 MoErv14 介导这些受体蛋白的转运，以促进米霉的附着胞形成和致病性。
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. During the pathogenic interaction with rice, Magnaporthe oryzae senses cell surface cues and forms a highly specialized infectious structure called an appressorium that initiates the infection. Studies have shown several transmembrane proteins essential for the perception of rice host cues. However, little is known about how these transmembrane proteins are trafficked intracellularly to impact appressorium formation and pathogenicity. In this study, we found MoErv14 is important in the growth and pathogenicity of the blast fungus, and MoErv14 regulates the transport of several membrane sensors, including MoPth11, MoWish, and MoSho1, that function upstream of either G-protein/cAMP signaling or the Pmk1-MAPK pathway. Importantly, we revealed that MoErv14 mediates the transport of these receptor proteins to promote the appressorium formation and pathogenicity of M. oryzae.
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