Abstract
The p53-related p63 gene encodes multiple protein isoforms, which are involved in a variety of biological activities. p63 protein stability is mainly regulated by the ubiquitin-dependent proteasomal degradation pathway. Several ubiquitin E3 ligases have been identified and some protein kinases as well as other kinds of proteins are involved in regulation of p63 protein stability. These regulators are responsive to diverse extracellular signaling, resulting in changes of the p63 protein levels and impacting different biological processes.
Highlights
The p53 family member, p63 gene, is located on human chromosome 3q27–29
Current studies reveal that p63 protein stability is tightly controlled and closely correlated with cell proliferation, cell death, and cell differentiation
The same residues or same regions are targeted by different E3 ligases or different signaling
Summary
The p53 family member, p63 gene, is located on human chromosome 3q27–29. In contrast to the high frequency of p53 mutations in cancers, p63 gene is rarely mutated [1, 2]. A vast body of evidence demonstrates that p63 are key transcription factors involved in cell growth, proliferation, apoptosis, and differentiation and play an essential role in epithelial stem cell biology and development [4,5,6,7,8] Due to their key roles in a variety of essential biological processes, abundances of p63 proteins are tightly controlled. Some important regulators, including ubiquitin E3 ligases, kinases, and proteins in other classes, have been reported to control p63 degradation. Multiple extracellular signalings, such as growth factor signaling and genotoxic stress, impact these regulators, which in turn modulate protein stability of p63 [9, 10]. This review is aimed at understanding the molecular mechanisms, by which p63 protein stability is regulated, and the players in modulating ubiquitin-dependent proteasomal degradation of p63 proteins
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