I think K "stabilizes" mutant p53 (via ubiquitination or phosphorylation), so that it builds up in the cytosol, interacts with BAX, and leads to mitochondrial driven apoptosis.
From Kumar 2011 AACR poster, "Immunoprecipitation and western blot experiments confirmed the induction of p53 monoubiquitination in response to Kevetrin. p53 monoubiquitination enhances the stability and accumulatino of p53 in the cytosol or mitochondria directly activating apoptosis."
"We found that stable monoubiquitinated mutant p53 was induced by Kevetrin."
Check out the Chipuk et al. 2004 Science paper, for details how even some mutant p53 can still function to cause apoptosis via BAX interaction:
"The induction of apoptosis is central to the tumor-suppressive activity of p53 (1). Upon activation by DNA damage–induced or oncogene-induced signaling pathways, p53 promotes the expression of a number of genes that are involved in apoptosis, including those encoding death receptors (2, 3) and proapoptotic members of the Bcl-2 family (4, 5). In most cases, p53-induced apoptosis proceeds through mitochondrial release of cytochrome c, which leads to caspase activation (6).
Although most of the effects of p53 are ascribed to its function as a transcription factor, reports have suggested that the protein can also induce apoptosis independently of new protein synthesis (7–10). However, these studies have relied on ectopic expression of p53 or overexpression of mutants that lack transcriptional activity. Transcription-independent induction of apoptosis by p53 requires Bax and involves cytochrome c release and caspase activation, all of which occur in the absence of a nucleus, suggesting that p53 has the capacity to engage the apoptotic program directly from the cytoplasm (11)."
"a stably expressed temperature-sensitive form of p53QS, localized to the cytosol, was reported to induce apoptosis upon stabilization (10). To test the direct cytoplasmic effects of p53 in the absence of p53-induced gene expression, p53UVIP, p53?PP (no proline-rich domain, amino acids 62 to 91), and p53QS were purified (fig. S3, A and B) and microinjected into HeLa cells"
"Thus, we examined the effect of p53 on isolated mitochondria with and without Bax. Neither recombinant monomeric Bax nor native p53UVIP induced cytochrome c release on its own; however, incubation of mitochondria with both proteins caused cytochrome c release (Fig. 2B)."
"The capacity of p53 to directly activate Bax to permeabilize mitochondria permits an uninterrupted pathway leading from DNA damage, for example, to the mitochondrial release of cytochrome c, caspase activation, and apoptosis. The previously unobserved function of p53, which is analogous to that of a BH3-only protein, in addition to its function as a transcription factor, demonstrates an emerging complexity that exists within components of the apoptotic machinery."
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