منابع مشابه
TRIMming p53 for ubiquitination.
T he function of the p53 tumor suppressor protein is finely tuned through a myriad of interactions with other proteins. These interactions can lead to posttranslational modifications that regulate p53 stability, DNA binding, or promoterspecific transcriptional activation. A number of p53 binding proteins serve as cofactors that participate in the recruitment of p53 to specific promoters and fac...
متن کاملA New Function for p53 Ubiquitination
The amount of p53 protein in a cell is normally limited by ubiquitin-dependent degradation. In this issue of Cell, Le Cam et al. (2006) reveal that p53 ubiquitination contributes to transcriptional activation rather than protein stability. These results may provide insight into how p53 can modulate diverse cellular processes such as growth arrest and apoptosis.
متن کاملUbiquitination of Bag-1
Intense apoptoses occur during the morphogenesis period of embryonic development. In the adult, and in the absence of genotoxic aggressions or degenerative pathologies, normal apoptoses strongly decrease in most organs and become restricted to self-renewing tissues containing progenitor stem cells, allowing continuous cell replacement. This is the case in the olfactory neuroepithelium that line...
متن کاملSUMO-1 Modification of Mdm2 Prevents Its Self-Ubiquitination and Increases Mdm2 Ability to Ubiquitinate p53
Mdm2 is an E3 ubiquitin ligase for the p53 tumor suppressor protein. We demonstrate that Mdm2 is conjugated with SUMO-1 (sumoylated) at Lys-446, which is located within the RING finger domain and plays a critical role in Mdm2 self-ubiquitination. Whereas mutant Mdm2(K446R) is stabilized, it elicits increased degradation of p53 and concomitant inhibition of p53-mediated apoptosis. In vitro sumoy...
متن کاملJNK targets p53 ubiquitination and degradation in nonstressed cells.
In this study we elucidated the role of nonactive JNK in regulating p53 stability. The amount of p53-JNK complex was inversely correlated with p53 level. A peptide corresponding to the JNK binding site on p53 efficiently blocked ubiquitination of p53. Similarly, p53 lacking the JNK binding site exhibits a longer half-life than p53(wt). Outcompeting JNK association with p53 increased the level o...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2009
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0905997106