Isoform specific phosphorylation of p53 by protein kinase CK1

The ability of three isoforms of protein kinase CK1 to phosphorylate the N-terminal region of p53 has been assessed using either recombinant p53 or a synthetic peptide reproducing its 1–28 sequence. Both substrates are readily phosphoylated by CK1δ and CK1α, but not by the γ isoform

Andrea Venerando

2009

Scholarcy highlights

  • The ability of three isoforms of protein kinase CK1 to phosphorylate the N-terminal region of p53 has been assessed using either recombinant p53 or a synthetic peptide reproducing its 1–28 sequence. Both substrates are readily phosphoylated by CK1δ and CK1α, but not by the γ isoform
  • The preferred target is S20, whose phosphorylation critically relies on E17, while S6 is unaffected despite displaying the same consensus
  • Our data support the concept that non-primed phosphorylation of p53 by CK1 is an isoform-specific reaction preferentially affecting S20 by a mechanism which is grounded both on a local consensus and on a remote docking site mapped to the K221RQK224 loop according to modeling and mutational analysis
  • Poletto G, Vilardell J, Marin O, Pagano MA, Cozza G, Sarno S, Falqués A, Itarte E, Pinna LA, Meggio F The regulatory beta subunit of protein kinase CK2 contributes to the recognition of the substrate consensus sequence

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