IndraLab
Statements
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"While Chk2 activates multiple downstream targets in addition to p53, and the p53 protein may be activated through multiple post-transcriptional events [ xref ], the finding that CHEK2 mutations may substitute for TP53 mutations as a cause of chemo-resistance indicates Chk2 phosphorylation of the p53 protein to play a pivotal role executing cell death in response to anthracycline therapy in breast cancer."
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"The phosphorylation of CHK2 and p53 was also increased by EEOM, indicating that activated CHK2 triggers p53 phosphorylation to increase the stability of p53. xref , xref However, EEOM did not show any big difference in the protein levels of Cdc25C. These results suggest that EEOM-mediated G2/M arrest occurs by inhibition of CDK/cyclin complex via p53-dependent p21 induction."
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"Several studies showed that DNA double-strand breaks induce phosphorylation of p53 S15 by ATM or DNA-PK. xref , xref ATM also activates Chk2, which in turn phosphorylates p53 on S20 which is part of the MDM2 binding site. xref , xref These findings suggested a model that p53 phosphorylation on the N terminus disrupts MDM2 binding and results in p53 stabilization."
"The tumour suppressor protein p53 is stabilised and activated in response to ionising radiation. This is known to depend on the kinase atm;recent results suggest atm acts via the downstream kinase chk2/hcds1, which stabilises p53 at least in part by direct phosphorylation of residue serine 20"
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"However, during the later stages, CHK2 may contribute to p53 phosphorylation at Ser366 and Ser378, resulting in p53 degradation through the ubiquitin-proteasome pathway and blocking of p53 mediated apoptosis [XREF_BIBR] and the EBV protein kinase BGLF4 contributes to p27 phosphorylation and its ubiquitin-proteasome dependent degradation [XREF_BIBR]."
"The cell cycle checkpoint kinases CHK1 and CHK2 have been shown to phosphorylate multiple sites in the N-terminal domain of p53, consequently leading to p53 stabilization and activation. Phosphorylation of at least three of these sites, Ser366, Ser378, and Thr387, was induced by DNA damage."
"The cell cycle checkpoint kinases CHK1 and CHK2 have been shown to phosphorylate multiple sites in the N-terminal domain of p53, consequently leading to p53 stabilization and activation. Phosphorylation of at least three of these sites, Ser366, Ser378, and Thr387, was induced by DNA damage."
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"However, during the later stages, CHK2 may contribute to p53 phosphorylation at Ser366 and Ser378, resulting in p53 degradation through the ubiquitin-proteasome pathway and blocking of p53 mediated apoptosis [XREF_BIBR] and the EBV protein kinase BGLF4 contributes to p27 phosphorylation and its ubiquitin-proteasome dependent degradation [XREF_BIBR]."
"The cell cycle checkpoint kinases CHK1 and CHK2 have been shown to phosphorylate multiple sites in the N-terminal domain of p53, consequently leading to p53 stabilization and activation. Phosphorylation of at least three of these sites, Ser366, Ser378, and Thr387, was induced by DNA damage. On activation, both of these kinases also phosphorylate multiple sites in the p53 N-terminal domain. These include Ser15, Thr18, Ser20, and Ser37, which are all DNA-damageinducible sites"
CHEK2 phosphorylated on S379, T383, T387, and T68 phosphorylates TP53 phosphorylated on S15 on S20. 1 / 1
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