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. 2015 Feb 15;26(4):805–820. doi: 10.1091/mbc.E14-08-1319

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© 2015 Sugden et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 6: — DIF-1 induced dephosphorylation of PKB homologues and their substrates. (A) Summary of DIF-1–regulated phosphorylation sites in PKBA, PKBR1, and their substrates. (B) Temporal profile for DIF-1–induced phosphorylation changes in class I sites on PKBA, PKBR1, and their substrate SHAPS (DDB0306661). Solid lines represent averaged data for class I sites and dashed lines are from class III sites from a single experiment. (C) Heat-map representation of the temporal phosphorylation changes of class I DIF-1–regulated phosphorylation sites in PKB substrates. Averaged values, n ≥ 2. (D) PKB AL phosphorylation in response to DIF-1. Ax2 cells starved for 5 h were treated ± 100 nM DIF-1. Results are representative of at least three independent experiments. (E) Antagonism between cAMP and DIF-1. Cells were starved as in D and then treated with 1 μM cAMP ± 100 nM DIF-1. Samples collected at the times indicated and then immunoblotted as in D. (F) The response of PKB substrate phosphorylation to DIF-1. Samples from D were immunoblotted with anti-phosphospecific PKB substrate antibody. Blots were stripped and reprobed with anti-actin antibody as a loading control.