Abstract
The p53 tumor suppressor protein is normally restrained by the Mdm2 oncoprotein, which promotes p53 ubiquitination. In a recent issue of Science, report that p53 may face two alternative fates, depending on Mdm2 levels: high Mdm2 drives p53 polyubiquitination and degradation within the cell nucleus, whereas low Mdm2 promotes p53 monoubiquitination and nuclear exclusion.
MeSH terms
-
Active Transport, Cell Nucleus
-
Apoptosis
-
Cell Nucleus / metabolism*
-
Cysteine Endopeptidases / metabolism
-
Cytoplasm / metabolism
-
Gene Expression Regulation*
-
Humans
-
Ligases
-
Models, Biological
-
Multienzyme Complexes / metabolism
-
Nuclear Proteins*
-
Proteasome Endopeptidase Complex
-
Proto-Oncogene Proteins / metabolism*
-
Proto-Oncogene Proteins c-mdm2
-
Recombinant Fusion Proteins / metabolism
-
Tumor Suppressor Protein p53 / genetics
-
Tumor Suppressor Protein p53 / metabolism*
-
Ubiquitin / genetics
-
Ubiquitin / metabolism
Substances
-
Multienzyme Complexes
-
Nuclear Proteins
-
Proto-Oncogene Proteins
-
Recombinant Fusion Proteins
-
Tumor Suppressor Protein p53
-
Ubiquitin
-
MDM2 protein, human
-
Proto-Oncogene Proteins c-mdm2
-
Cysteine Endopeptidases
-
Proteasome Endopeptidase Complex
-
Ligases