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Ubiquitin-independent p53 proteasomal degradation Tsvetkov P; Reuven N; Shaul YCell Death Differ 2010[Jan]; 17 (1): 103-8The mechanism of p53 proteasomal degradation through polyubiquitination is well characterized. The basic assumption behind this mechanism is that p53 is inherently stable unless sensitized to degradation by polyubiquitination. However, a number of studies provide evidence for p53 to be naturally unstable. Consistent with this attribute is the fact that both p53 N- and C-termini are intrinsically unstructured. Recent findings provide evidence for p53 to be degraded by the 20S proteasome by default unless it escapes this process. A number of mechanisms were demonstrated and proposed to play a role in rescuing p53 from default degradation. These mechanisms, their biological implications, and relevance to cancer are reviewed in this article.|Humans[MESH]|NAD(P)H Dehydrogenase (Quinone)/metabolism[MESH]|Proteasome Endopeptidase Complex/*metabolism[MESH]|Tumor Suppressor Protein p53/*metabolism[MESH]|Ubiquitin/*metabolism[MESH] |