Direct interaction of the beta-domain of VHL tumor suppressor protein with the regulatory domain of atypical PKC isotypes.
VHL tumor suppressor protein contains two domains, alpha and beta. The alpha-domain is involved in the formation of a large protein complex suggested to be involved in ubiquitin-mediated protein degradation. However, the role of the beta-domain, which may recognize the target proteins for protein degradation, remains unknown. Here we report ... that the beta-domain interacts directly with atypical PKC isotypes, PKCzeta and PKClambda. Further, the regulatory domain of aPKC is sufficient for this direct protein-protein interaction. Since aPKC isotypes have been implicated in the regulation of cell growth and apoptosis, these results suggest that aPKC isotypes are potential direct target of the VHL beta-domain.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Cells, Cultured, Genes, Tumor Suppressor, Humans, Isoenzymes, Kidney, Ligases, Molecular Sequence Data, Peptide Fragments, Precipitin Tests, Protein Binding, Protein Kinase C, Proteins, Recombinant Proteins, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Von Hippel-Lindau Tumor Suppressor Protein
Amino Acid Sequence, Binding Sites, Cells, Cultured, Genes, Tumor Suppressor, Humans, Isoenzymes, Kidney, Ligases, Molecular Sequence Data, Peptide Fragments, Precipitin Tests, Protein Binding, Protein Kinase C, Proteins, Recombinant Proteins, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Von Hippel-Lindau Tumor Suppressor Protein
Biochem. Biophys. Res. Commun.
Date: Sep. 24, 1999
PubMed ID: 10491320
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