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. 2020 May 13;39(13):e103695. doi: 10.15252/embj.2019103695

Figure 3. Differential phosphorylation site preference of PP2A‐B56 and PP2A‐B55.

Figure 3

  • A
    Michaelis–Menten kinetic parameters of purified PP2A‐B56α and PP2A‐B55α holoenzymes were determined against the indicated phosphopeptides. Mean and standard deviation shown in plots as black bars (n = 3 independent experiments).
  • B–D
    In vitro dephosphorylation by the PP2A‐B55α and PP2A‐B56α holoenzymes of panels of phosphorylated peptides as indicated. Mean and standard deviation shown in plots as black bars (n = 3 independent experiments).