Degrading mutant p53 would seem incongruous. What would be simulating the activity of wild type p53 in the cell in the absence of the mutant p53? You must either be mutant or not -- there are not generally competing populations of mutant and wild type in the cell, since the source of protein must come from the single transcribable DNA source which is either mutated or not. So if you degrade mutant p53, you would simply have no p53 function whatsoever and thus no regulation OR G2 arrest OR p53 mediated apoptosis. Thus, degrading p53 would simply not yield anything beneficial in my interpretation of things. Therefore, if Kevetrin is an effective modulator of serine-15 phosphorylation which, in its phosphoryl-activated form triggers G2 arrest and apoptosis, this can only logically be the pure effect of the small molecule on protein folding to expose the serine R-group or in some other way facilitate serine-15 phosphorylation to return mutant p53 to its activated state. Addressing or characterizing this drug's activity as "degradation of mutant p53" just doesn't seem like it would translate to anything useful in terms of the system.
Dr. Jeremy Durchman
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