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Calcineurin Is an Antagonist to PKA Protein Phosphorylation Required for Postmating Filamentation and Virulence, While PP2A Is Required for Viability in Ustilago maydis

October 2009 , Volume 22 , Number  10
Pages  1,293 - 1,301

John D. Egan,1 María D. García-Pedrajas,2 David L. Andrews,1 and Scott E. Gold1

1Department of Plant Pathology, University of Georgia, Athens, GA 30602-7274, U.S.A.; 2Estación Experimental “La Mayora”, CSIC, 29760 Algarrobo-Costa, Málaga, Spain

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Accepted 25 May 2009.

Ustilago maydis is a dimorphic basidiomycete and the causal agent of corn smut disease. It serves as a genetic model for understanding dimorphism, pathogenicity, and mating response in filamentous fungi. Previous studies indicated the importance of regulated cAMP-dependent protein kinase A (PKA) for filamentous growth and pathogenicity in U. maydis. The roles of two protein phosphatases that potentially act antagonistically to PKA were assessed. A reverse genetics approach to mutate the catalytic subunits of calcineurin (CN, protein phosphatase [PP]2B) and PP2A in U. maydis was employed. A mutation in the CN catalytic subunit ucn1 caused a dramatic multiple-budding phenotype and mating between two ucn1 mutants was severely reduced. The pathogenicity of ucn1 mutant strains was also severely reduced, even in a solopathogenic haploid strain. Importantly, mutations disrupting protein phosphorylation by PKA were epistatic to ucn1 mutation, indicating a major role of ucn1 as a PKA antagonistic phosphatase. Genetic and inhibitor studies indicated that the U. maydis PP2A catalytic subunit gene (upa2) was essential.

© 2009 The American Phytopathological Society