Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C.
Germ-line mutations of the von Hippel-Lindau tumor suppressor gene (VHL) predispose individuals to a variety of human tumors, and somatic mutations of this gene have been identified in sporadic renal cell carcinomas and cerebellar hemangioblastomas. Two transcriptional elongation factors, Elongin B and C, were shown to bind in vitro and ... in vivo to a short, colinear region of the VHL protein (pVHL) that is frequently mutated in human tumors. A peptide replica of this region inhibited binding of pVHL to Elongin B and C whereas a point-mutant derivative, corresponding to a naturally occurring VHL missense mutation, had no effect. These results suggest that the tumor suppression function of pVHL may be linked to its ability to bind to Elongin B and C.
Mesh Terms:
Amino Acid Sequence, Animals, Carcinoma, Renal Cell, Genes, Tumor Suppressor, Germ-Line Mutation, Humans, Ligases, Mice, Molecular Sequence Data, Nuclear Proteins, Point Mutation, Recombinant Fusion Proteins, Transcription Factors, Transfection, Tumor Cells, Cultured, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Von Hippel-Lindau Tumor Suppressor Protein, von Hippel-Lindau Disease
Amino Acid Sequence, Animals, Carcinoma, Renal Cell, Genes, Tumor Suppressor, Germ-Line Mutation, Humans, Ligases, Mice, Molecular Sequence Data, Nuclear Proteins, Point Mutation, Recombinant Fusion Proteins, Transcription Factors, Transfection, Tumor Cells, Cultured, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, Von Hippel-Lindau Tumor Suppressor Protein, von Hippel-Lindau Disease
Science
Date: Sep. 08, 1995
PubMed ID: 7660130
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