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KMID : 0380020090240030217
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Korean Journal of Biotechnology and Bioengineering
2009 Volume.24 No. 3 p.217 ~ p.226
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Regulation of cellular functions of p53 by ubiquitination
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Jung Jin-Hyuk
Lee Joon-Young
Lee Sun-Mi
Choe Tae-Boo
An Sung-Kwan
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Abstract
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p53 undergoes various post-translational modifications, including phosphorylation, ubiquitination, sumoylation, acetylation, methylation, and poly(ADP-ribosyl)ation. Modification of p53 widely affects to various functions of p53. Acetylation and phosphorylation of p53 have been studied for regulating its transcriptional activity which is observed in various stress condition. Otherwise, ubiquitination of p53 by Mdm2 has been well-studied as a canonical ubiquitin-mediated proteasomal degradation pathway. Moreover several investigators have recently reported that ubiquitination of p53 modulates not only its proteasome-dependent degradation by poly-ubiquitination but also its localization and transcriptional activity by mono-ubiquitination which usually does not serve the proteasome dependent degradation. Here we review recent studies on the cellular functions of p53 regulated by post-translational modifications, particularly focusing on mechanisms of ubiquitination.
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KEYWORD
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p53, ubiquitin-mediated degradation, localization, modulation of transcriptional activity
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