ROS promote the activation of c-Jun N-terminal kinase (JNK) and DNA damage response, which establishes a positive feedback loop with p53. This converts the p53-induced growth arrest/senescence to apoptosis.

2014年1月10日 · ROS promote the activation of c-Jun N-terminal kinase (JNK) and DNA damage response, which establishes a positive feedback loop with p53. This converts the p53-induced growth...

Activation of the tumor suppressor p53 by stress and damage stimuli often correlates with induction of stress kinases, Jun-NH2 kinase (JNK). As JNK association with p53 plays an important role in p53 stability, in the present study we have ...

2005年1月1日 · The anti-apoptotic function of JNK may be related to the status of p53 since JNKAS inhibited growth of certain p53-deficient, but not p53 positive, tumor cells 55.

1998年9月9日 · In this study we elucidated the role of nonactive JNK in regulating p53 stability. The amount of p53–JNK complex was inversely correlated with p53 level. A peptide corresponding to the JNK binding site on p53 efficiently blocked ubiquitination of p53.

2012年1月20日 · Our study unveils a previously undescribed mechanism of RITA-induced p53-mediated apoptosis through JNK signaling pathway and provides the rationale for combination of p53 activating drugs with JNK activators in the treatment of MM.

2014年4月15日 · Here we report that 5-FU treatment causes aberrant autophagosome accumulation in HCT116 p53 (-/-) and HT-29 cancer cells. Specific inhibition of autophagy by 3-MA, CQ or small interfering RNA treatment targeting Atg5 or Beclin 1 can potentiate the re-sensitization of these resistant cancer cells to 5-FU.

2024年10月15日 · As downstream of intracellular enzyme JNK, c-Jun negatively regulates the transcription of p53 through the transcription factor AP-1 during cell cycle progression (Schreiber et al., 1999; Zeke et al., 2016). This study employed a JNK inhibitor to investigate JNK/P53 signaling in hepatocytes under heat stress.

2018年4月3日 · We found that JNK-mediated phosphorylation of Thr 81 in the proline-rich domain (PRD) of p53 enabled wild-type p53, as well as mutant p53, to form a complex with p73. Structural algorithms predicted that phosphorylation of Thr 81 exposes the DNA-binding domain in p53 to enable its binding to p73.

The activation of MAP kinase JNK upon inhibition of TrxR 29 and its ability to modulate p53 make JNK an attractive candidate mediator of ROS signaling to p53. We found that RITA induced JNK phosphorylation (p-JNK) in a p53- and dose-dependent manner (Figures 4a and b).