Binding of the von Hippel-Lindau Tumor Suppressor Protein to Elongin B and C
- 8 September 1995
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 269 (5229) , 1444-1446
- https://doi.org/10.1126/science.7660130
Abstract
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.Keywords
This publication has 19 references indexed in Scilit:
- Elongin (SIII): A Multisubunit Regulator of Elongation by RNA Polymerase IIScience, 1995
- Inhibition of Transcription Elongation by the VHL Tumor Suppressor ProteinScience, 1995
- Characterization of the VHL tumor suppressor gene product: localization, complex formation, and the effect of natural inactivating mutations.Proceedings of the National Academy of Sciences, 1995
- Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: Correlations with phenotypeHuman Mutation, 1995
- A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIIIGene, 1994
- Somatic mutations of the von Hippel — Lindau disease tumour suppressor gene in non-familial clear cell renal carcinomaHuman Molecular Genetics, 1994
- Identification of intragenic mutations in the Von Hippel — Lindau disease tumour suppressor gene andcorrelation with disease phenotypeHuman Molecular Genetics, 1994
- Internal protein sequence analysis: Enzymatic digestion for less than 10 μg of protein bound to polyvinylidene difluoride or nitrocellulose membranesAnalytical Biochemistry, 1992
- SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility geneCell, 1988
- Rapid site-specific mutagenesis in plasmidsGene, 1987