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• W2123676989 abstract "The Cdc25C phosphatase is a key regulator of mitotic entry which activity is tightly regulatedby phosphorylation. In response to DNA damage, phosphorylation at serine 216 induces thecytosolic retention of Cdc25C through 14-3-3 binding. We previously reported the ability ofthe p14ARF tumor suppressor to induce the accumulation of inactive phospho-Cdc25C(Ser216)protein as well as a decrease of Cdc25C steady state level and correlated these events with ap53-independent G2 arrest. The aim of this study was to investigate the cellular signalingpathways involved in this process. By using specific pharmacological inhibitors, wedemonstrate that activation of the ERK1/2 MAP kinases pathway is involved in the p53-independent G2 checkpoint induced by p14ARF. Moreover, we show that activated P-ERK1/2bind and phosphorylate Cdc25C on its ser216 residue following p14ARF expression, therebyidentifying Cdc25C as a new ERK1/2 target. Importantly, we further show thatphosphorylation at Ser216 by phospho-ERK1/2 promotes Cdc25C ubiquitination andproteasomal degradation, suggesting that Cdc25C proteolysis is required for a sustained G2arrest in response to p14ARF. Taken together, these results demonstrate that the MAPK ERKsignaling pathway contributes to the p53-independent antiproliferative functions of p14ARF.Furthermore, they identify a new mechanism by which phosphorylation at serine 216participates to Cdc25C inactivation." @default.
• W2123676989 created "2016-06-24" @default.
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• W2123676989 date "2006-03-23" @default.
• W2123676989 modified "2023-09-25" @default.
• W2123676989 title "p14ARF Triggers G2 Arrest Through ERK-Mediated Cdc25C Phosphorylation, Ubiquitination and Proteasomal Degradation" @default.
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• W2123676989 doi "https://doi.org/10.4161/cc.5.7.2625" @default.
• W2123676989 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16582626" @default.
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