PP2C phosphatases Ptc1 and Ptc2 dephosphorylate PGK1 to regulate autophagy and aflatoxin synthesis in the pathogenic fungus Aspergillus flavus

• Published in: mBio Vol. 14; no. 5; p. e0097723
• Main Authors: Zhu, Zhuo, Yang, Mingkun, Yang, Guang, Zhang, Bei, Cao, Xiaohong, Yuan, Jun, Ge, Feng, Wang, Shihua
• Format: Journal Article
• Language: English
• Published: United States American Society for Microbiology 31.10.2023
• Subjects: aflatoxin; Aflatoxins - metabolism; Aspergillus flavus; Aspergillus flavus - metabolism; Autophagy; IP-MS; phosphoglycerate kinase 1; Phosphoric Monoester Hydrolases - metabolism; Plant Microbiology; PP2C phosphatase; Protein Phosphatase 2C - genetics; Protein Phosphatase 2C - metabolism; Research Article; PP2C phosphatase; phosphoglycerate kinase 1; Aspergillus flavus; aflatoxin; IP-MS
• ISSN: 2150-7511; 2150-7511
• DOI: 10.1128/mbio.00977-23

is a model filamentous fungus that can produce aflatoxins when it infects agricultural crops. This study evaluated the protein phosphatase 2C (PP2C) family as a potential drug target with important physiological functions and pathological significance in . We found that two redundant PP2C phosphatases, Ptc1 and Ptc2, regulate conidia development, aflatoxin synthesis, autophagic vesicle formation, and seed infection. The target protein phosphoglycerate kinase 1 (PGK1) that interacts with Ptc1 and Ptc2 is essential to regulate metabolism and the autophagy process. Furthermore, Ptc1 and Ptc2 regulate the phosphorylation level of PGK1 S203, which is important for influencing aflatoxin synthesis. Our results provide a potential target for interdicting the toxicity of .