A novel p53-binding domain in CUL7.
CUL7 is a member of the cullin RING ligase family and forms an SCF-like complex with SKP1 and FBXW8. CUL7 is required for normal mouse embryonic development and cellular proliferation, and is highly homologous to PARC, a p53-associated, parkin-like cytoplasmic protein. We determined that CUL7, in a manner similar to ... PARC, can bind directly to p53 but does not affect p53 expression. We identified a discrete, co-linear domain in CUL7 that is conserved in PARC and HERC2, and is necessary and sufficient for p53-binding. The presence of p53 stabilized expression of this domain and we demonstrate that this p53-binding domain of CUL7 contributes to the cytoplasmic localization of CUL7. The results support the model that p53 plays a role in regulation of CUL7 activity.
Mesh Terms:
Animals, Binding Sites, Carrier Proteins, Cell Line, Tumor, Cells, Cultured, Cullin Proteins, Humans, Mice, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases
Animals, Binding Sites, Carrier Proteins, Cell Line, Tumor, Cells, Cultured, Cullin Proteins, Humans, Mice, Protein Binding, Protein Structure, Tertiary, Sequence Homology, Tumor Suppressor Protein p53, Ubiquitin-Protein Ligases
Biochem. Biophys. Res. Commun.
Date: Sep. 15, 2006
PubMed ID: 16875676
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