Fig. 9: Snf1 and Pp4 regulate each other's phosphorylation status in Magnaporthe oryzae. | Communications Biology

Fig. 9: Snf1 and Pp4 regulate each other's phosphorylation status in Magnaporthe oryzae.

From: A multilayered regulatory network mediated by protein phosphatase 4 controls carbon catabolite repression and de-repression in Magnaporthe oryzae

Fig. 9

a Yeast two-hybrid analysis of Snf1 with Smek1 and Pp4c. GST pull-down (b) and co-immunoprecipitation (d) assays to confirm Snf1 interaction with Pp4c. GST pull-down (c) and co-immunoprecipitation (e) assays to confirm Snf1 interaction with Smek1. Strains were cultured in glucose medium for 2 days (d, e). f Mn2+ phos-tag assays demonstrating Snf1 phosphorylation of Pp4c but not Smek1 in vivo. g Schematic of Snf1-mediated phosphorylation of Pp4c and Crf1, with subsequent Pp4c-mediated dephosphorylation of CreA and Crf1. Western blot of Snf1 phosphorylation levels in the wild-type, Δpp4c, and Δsmek1 strains cultured in glucose and l-arabinose media: representative images (h), and statistical graphs (i). Error bars represent SD. Asterisks “**” indicate significant differences (Tukey's HSD test, p < 0.01). n = 5 biologically independent samples. j Diagram illustrating Snf1 dephosphorylation by Pp4c and Smek1.

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