Suppression of the Deubiquitinating Enzyme USP5 Causes the Accumulation of Unanchored Polyubiquitin and the Activation of p53

Both p53 and its repressor Mdm2 are subject to ubiquitination and proteasomal degradation. We show that knockdown of the deubiquitinating enzyme USP5 (isopeptidase T) results in an increase in the level and transcriptional activity of p53. Suppression of USP5 stabilizes p53, whereas it has little or...

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Veröffentlicht in:	The Journal of biological chemistry 2009-02, Vol.284 (8), p.5030-5041
Hauptverfasser:	Dayal, Saurabh, Sparks, Alison, Jacob, Jimmy, Allende-Vega, Nerea, Lane, David P., Saville, Mark K.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Substitution Cancer Cell Line, Tumor Endopeptidases - genetics Endopeptidases - metabolism Enzymes Gene Knockdown Techniques Humans MDM2 protein Mutation, Missense p53 protein Proteasome Endopeptidase Complex - genetics Proteasome Endopeptidase Complex - metabolism proteasomes Proto-Oncogene Proteins c-mdm2 - genetics Proto-Oncogene Proteins c-mdm2 - metabolism Repressors Transcription activation Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism Ubiquitin Ubiquitin - genetics Ubiquitin - metabolism ubiquitination Ubiquitination - physiology
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