Identification of β-catenin as a novel substrate of polo-like kinase 1
| Autor: | Masato Iida, Yuko Iimura-Morita, Tsuyoshi Arai, Kyosuke Haze, Hideya Komatani, Kenji Tanaka, Takumitsu Machida |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Small interfering RNA
Gene Expression Cell Cycle Proteins Protein Serine-Threonine Kinases Biology PLK1 Cell Line Substrate Specificity Phosphorylation cascade MAP2K7 Proto-Oncogene Proteins Serine Humans Protein phosphorylation Phosphorylation Molecular Biology beta Catenin MAPK14 Kinase Cell Cycle Cell Biology Cell biology enzymes and coenzymes (carbohydrates) Biochemistry Cell Division Protein Binding Developmental Biology |
| Zdroj: | Cell Cycle. 7:3556-3563 |
| ISSN: | 1551-4005 1538-4101 |
| DOI: | 10.4161/cc.7.22.7072 |
| Popis: | Polo-like kinase 1 (Plk1) is a serine/threonine kinase that plays an important role in M phase progression by regulating various downstream substrates via phosphorylation. Here, we identified beta-catenin as a novel substrate of Plk1 and determined that Ser-718 is a phosphorylation site for Plk1 by using a phospho-specific antibody that cross-reacts with Plk1-dependent phosphorylation sites. Ser-718 of beta-catenin was directly phosphorylated by recombinant Plk1 in vitro, with the phosphorylation signal in cells increasing with overexpression of Plk1 and decreasing when endogenous Plk1 was depleted by small interfering RNA. The phosphorylation at Ser-718 was correlated with the cell cycle-dependent expression of Plk1 which reached a maximum in M phase. We also confirmed that there is a physical interaction between beta-catenin and Plk1 using coimmunoprecipitation and a GST pull-down assay. These results demonstrate that beta-catenin is a physiological substrate of Plk1 in cells, which may provide a novel insight into the role of beta-catenin in M phase. |
| Databáze: | OpenAIRE |
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