Protein -palmitoylation, a universal posttranslational modification catalyzed by a specific group of palmitoyltransferases, plays crucial roles in diverse biological processes across organisms by modulating protein functions. However, its roles in the virulence of plant pathogenic fungi remain underexplored. In a recent study, Y. Duan, P. Li, D. Zhang, L. Wang, et al. (mBio 15:e02704-24, 2024, https://doi.org/10.1128/mbio.02704-24) reported that the palmitoyltransferases UvPfa3 and UvPfa4 regulate the virulence of the rice false smut pathogen . Through comprehensive characterization of -palmitoylation sites, they revealed that -palmitoylated proteins in are enriched in mitogen-activated protein (MAP) kinase and autophagy pathways, with MAP kinase UvSlt2 being a key target of UvPfa4-mediated -palmitoylation. Further investigation demonstrated that -palmitoylation of UvSlt2 is critical for its kinase activity, substrate interaction ability, and virulence function in . These findings reveal UvPfa4-mediated -palmitoylation as a vital regulatory mechanism in virulence, highlighting the importance of protein -palmitoylation in the pathogenicity of plant pathogenic fungi.
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http://dx.doi.org/10.1128/mbio.03472-24 | DOI Listing |
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