Related Experiment Video
Updated: Jul 30, 2025

Visualizing Early Infection Sites of Rice Blast Disease Magnaporthe oryzae on Barley Hordeum vulgare Using a Basic Microscope and a Smartphone
Published on: March 17, 2023
Hydrophobic cue-induced appressorium formation depends on MoSep1-mediated MoRgs7 phosphorylation and internalization
Jiayun Xu1,2, Xinyu Liu1,2, Wei Zhang1,2
1Department of Plant Pathology, College of Plant Protection, Nanjing Agricultural University, and Key Laboratory of Integrated Management of Crop Diseases and Pests, Ministry of Education, Nanjing, China.
Abstract:
The rice blast fungus Magnaporthe oryzae forms specialized infectious structures called appressoria that breach host cells to initiate infection. Previous studies demonstrated that the regulator of G-protein signaling (RGS)-like protein MoRgs7 undergoes endocytosis upon fungal sensing of hydrophobic environmental cues to activate cAMP signaling required for appressorium formation. However, the mechanism by which MoRgs7 internalizes and its fate remains undetermined. We here show that MoSep1, a conserved protein kinase of Mitotic Exit Network (MEN), phosphorylates MoRgs7 to regulate its function. MoRgs7 phosphorylation determines its interaction with MoCrn1, a coronin-like actin-binding protein homolog that also modulates the internalization of MoRgs7. Importantly, the endocytic transport of MoRgs7 is critical for its GTPase-activating protein (GAP) function important in cAMP signaling. Together, our findings revealed a novel mechanism by which M. oryzae activates MoRgs7-mediated hydrophobic cue-sensing signal transduction involving protein phosphorylation and endocytic transport to govern appressorium formation and fungal pathogenicity.
Insights
The rice blast fungus uses protein phosphorylation and endocytosis to form appressoria. This process, involving MoSep1 and MoCrn1, is crucial for fungal infection and pathogenicity.
Area of Science:
- * Plant pathology
- * Molecular biology
- * Fungal genetics
Background:
- * Magnaporthe oryzae forms appressoria to infect rice plants.
- * The RGS-like protein MoRgs7 is essential for appressorium formation via endocytosis and cAMP signaling.
- * The precise mechanism of MoRgs7 internalization and its regulatory pathway were previously unknown.
Purpose of the Study:
- * To elucidate the mechanism of MoRgs7 internalization and its role in fungal pathogenicity.
- * To identify proteins involved in MoRgs7 regulation and endocytic transport.
- * To understand how hydrophobic cue sensing is transduced to regulate appressorium formation.
Main Methods:
- * Investigated the role of Mitotic Exit Network (MEN) kinase MoSep1 in MoRgs7 regulation.
- * Analyzed the interaction between MoRgs7 and coronin-like protein MoCrn1.
- * Studied the impact of MoRgs7 phosphorylation and endocytic transport on its GTPase-activating protein (GAP) function.
Main Results:
- * MoSep1 phosphorylates MoRgs7, influencing its interaction with MoCrn1.
- * MoCrn1 modulates the internalization of MoRgs7.
- * Endocytic transport of MoRgs7 is vital for its GAP activity in cAMP signaling.
Conclusions:
- * A novel mechanism involving MoSep1-mediated phosphorylation and MoCrn1-dependent endocytosis regulates MoRgs7.
- * This pathway is critical for hydrophobic cue sensing, cAMP signaling, appressorium formation, and pathogenicity in M. oryzae.
- * Findings provide new insights into signal transduction controlling fungal infection processes.
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