By R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner
This ultimate quantity within the sequence makes a speciality of malfunctions of the ubiquitin-proteasome procedure and their position in human disease.The editors and authors signify unrivaled services, comprising nearly the entire best scientists within the box, together with the pioneers of protein degradation research.From the contents:Ubiquitin and cancerUbiquitin and liver cancerMuscle atrophyAggresomes and human diseaseParkin and neurodegenerationChronic neurodegenerative diseasesParkinson's diseaseUbiquitin and virusesDruggability of the ubiquitin-proteasome systemRequired examining for molecular and cellphone biologists, in addition to physiologists with an curiosity within the subject.
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Extra info for Protein Degradation, Volume 4: The Ubiquitin-Proteasome System and Disease
Sample text
9 NEDD8/Rub1 NEDD8 shares the greatest homology with ubiquitin amongst the family of ubiquitin-like molecules. However, a distinct set of enzymatic activities are involved in 33 34 2 Regulation of the p53 Tumor-suppressor Protein by Ubiquitin and Ubiquitin-like Molecules NEDD8 modification of substrate proteins. Genetic experiments in yeast, plants, C. elegans, Drosophila and mice have shown an important role for NEDD8 in cell cycle and cell viability [178–181]. However, up until recently the only well-described substrate for NEDDylation was the cullin family of proteins.
Biochemical studies showed that ARF was able to inhibit the E3-ligase activity of Mdm2 [113, 114]. Further in vivo studies showed that ARF has a differential role in controlling the ligase activity of Mdm2. Blockade of the proteasomal degradation of p53 and Mdm2 by ARF was accompanied by the inhibition of p53 ubiqutination but not Mdm2 auto-ubiquitination [115]. Mdm2 contains a cryptic nucleolar sequence at the C-terminus (amino acids 466–473) which becomes exposed on interaction with ARF. Mutation of this signal makes Mdm2 resistant to nucleolar localization when ARF is bound [116].
This modification required the C-terminus of p53 but in contrast to ubiquitin a p53 mutant with three lysines in that domain (K370, K372, K373) mutated into arginine, was deficient in Mdm2-mediated NEDDylation. The role of NEDD8 in the control of p53 function was assessed in the TS41 system. These Chinese Hamster Ovary (CHO) cells carry a temperature sensitive mutation in the APP-BP1 gene (one of the components of the NEDD8 E1-activating enzyme; see above) [183]. When these cells were grown at restrictive temperatures (where the pathway is switched off) the transcriptional activity of p53 was increased.