Title : Arsenic trioxide reactivates proteasome-dependent degradation of mutant p53 protein in cancer cells in part via enhanced expression of Pirh2 E3 ligase.

Pub. Date : 2014

PMID : 25116336






6 Functional Relationships(s)
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1 Arsenic trioxide reactivates proteasome-dependent degradation of mutant p53 protein in cancer cells in part via enhanced expression of Pirh2 E3 ligase. Arsenic Trioxide tumor protein p53 Homo sapiens
2 Previously, we found that arsenic trioxide (ATO), a drug for acute promyelocytic leukemia, degrades mutant p53 protein through a proteasome pathway. Arsenic Trioxide tumor protein p53 Homo sapiens
3 Previously, we found that arsenic trioxide (ATO), a drug for acute promyelocytic leukemia, degrades mutant p53 protein through a proteasome pathway. Arsenic Trioxide tumor protein p53 Homo sapiens
4 We also found that knockdown of Pirh2 inhibits, whereas ectopic expression of Pirh2 enhances, ATO-induced degradation of mutant p53 protein. Arsenic Trioxide tumor protein p53 Homo sapiens
5 Interestingly, we found that ATO cooperates with HSP90 or HDAC inhibitor to promote mutant p53 degradation and growth suppression in tumor cells. Arsenic Trioxide tumor protein p53 Homo sapiens
6 Together, these data suggest that ATO promotes mutant p53 degradation in part via induction of the Pirh2-dependent proteasome pathway. Arsenic Trioxide tumor protein p53 Homo sapiens