*Plk1 is shown to phosphorylate Wee1A, an event that is likely critical for recognition and ubiquitination of Wee1A by SCF and therefore for the subsequent degradation of Wee1A . **Plk1 phosphorylates Wee1A at S53, creating the second phosphodegron, PD53. ** Evidence also exists in budding yeast that the budding yeast polo homolog Cdc5 directly phosphorylates and down-regulate the budding yeast Wee1 ortholog Swe1. Thus, polo kinase-dependent phosphorylation and degradation of Wee1A (or Swe1) is likely conserved throughout evolution and is critical for normal mitotic entry.
Nishihara, Y, Taniguchi, M, Arai, H, Watanabe, N, Osada, H, Hunter, T, Watanabe, N
Park, JE, Lee, KS, Veenstra, TD, Cho, YW, Sakchaisri, K, Yu, LR, Asano, S, Park, CJ, Shulewitz, MJ, Thorner, J
protein serine/threonine kinase activity of p-T210-PLK1 [nucleoplasm]
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