Endoplasmic reticulum/cytosolic localization of von hippel-lindau gene products is mediated by a 64-amino acid region

International Journal of Cancer

Volumn 91, Issue 4, 2001, Pages 457-467

  Schoenfeld, Alan R ^a   Davidowitz, Eliot J ^a   Burk, Robert D ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Endoplasmic reticulum; Renal cell carcinoma; Subcellular localization; Ubiquitination; Von Hippel Lindau (VHL)

Indexed keywords

AMINO ACID; CELL PROTEIN; GENE PRODUCT;

ANIMAL CELL; ARTICLE; CANCER INHIBITION; CELL FRACTIONATION; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOSOL; DISEASE ASSOCIATION; ENDOPLASMIC RETICULUM; FAMILIAL CANCER; GENE DELETION; GENE LOCATION; GENE MUTATION; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; KIDNEY CARCINOMA; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; TUMOR SUPPRESSOR GENE; VON HIPPEL LINDAU DISEASE;

ANIMALS; COS CELLS; CYTOSOL; ENDOPLASMIC RETICULUM; FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT; GENE DELETION; GREEN FLUORESCENT PROTEINS; HUMANS; KIDNEY; KIDNEY NEOPLASMS; LIGASES; LUMINESCENT PROTEINS; MICROSCOPY, CONFOCAL; MODELS, GENETIC; MUTATION; PLASMIDS; PROTEIN BIOSYNTHESIS; PROTEINS; RECOMBINANT FUSION PROTEINS; SUBCELLULAR FRACTIONS; TRANSFECTION; TUMOR CELLS, CULTURED; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN-PROTEIN LIGASES; UBIQUITINS; VON HIPPEL-LINDAU TUMOR SUPPRESSOR PROTEIN;

EID: 0035865958     PISSN: 00207136     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0215(20010215)91:4<457::AID-IJC1072>3.0.CO;2-P     Document Type: Article

References (44)

1. Clinical features and natural history of von Hippel-Lindau disease
2. Identification of the von Hippel-Lindau disease tumor suppressor gene
3. Identification of intragenic mutations in the von Hippel-Lindau disease tumour suppressor gene and correlation with disease phenotype
4. Germ-line mutations in the von Hippel-Lindau tumor-suppressor gene are similar to somatic von Hippel-Lindau aberrations in sporadic renal cell carcinoma
5. Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: Correlations with phenotype
6. Identification of the von Hippel-Lindau (VHL) gene. Its role in renal cancer
7. Mutations of the VHL tumour suppressor gene in renal carcinoma
8. Somatic mutations of the von Hippel-Lindau tumor suppressor gene in sporadic central nervous system hemangioblastomas
9. Loss of heterozygosity and somatic mutations of the VHL tumor suppressor gene in sporadic cerebellar hemangioblastomas
10. Allelic deletions of the VHL gene detected in multiple microscopic clear cell renal lesions in von Hippel-Lindau disease patients
11. Tumor suppression by the human von Hippel-Lindau gene product
12. A second major native von Hippel-Lindau gene product, initiated from an internal translation start site, functions as a tumor suppressor
13. pVHL19 is a biologically active product of the von Hippel-Lindau gene arising from internal translation initiation
14. Alternate choice of initiation codon produces a biologically active product of the von Hippel Lindau gene with tumor suppressor activity
15. Characterization of the VHL tumor suppressor gene product: Localization, complex formation, and the effect of natural inactivating mutations
16. Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density
17. The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix
18. Subcellular localization of the von Hippel-Lindau disease gene product is cell cycle-dependent
19. Transcription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor protein
20. Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein
21. Post-transcriptional regulation of vascular endothelial growth factor mRNA by the product of the VHL tumor suppressor gene
22. Hypoxia-inducible protein binding to vascular endothelial growth factor mRNA and its modulation by the von Hippel-Lindau protein
23. Reversion of deregulated expression of vascular endothelial growth factor in human renal carcinoma cells by von Hippel-Lindau tumor suppressor protein
24. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
25. Inhibition of transcription elongation by the VHL tumor suppressor protein
26. Binding of the von Hippel-Lindau tumor suppressor protein to elongin B and C
27. Elongin (SIII): A multisubunit regulator of elongation by RNA polymerase II
28. The elongin BC complex and the von Hippel-Lindau tumor suppressor protein
29. The elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families
30. Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog
31. Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2
32. The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
33. Rbxl, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase
34. The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity
35. Identification of the von Hippel-Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
36. SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box
37. Protective function of von Hippel-Lindau protein against impaired protein processing in renal carcinoma cells
38. Localization of endoplasmic reticulum in living and glutaraldehyde-fixed cells with fluorescent dyes
39. Site-directed mutations of the FAD-linked glycerophosphate dehydrogenase gene impairs the mitochondrial anchoring of the enzyme in transfected COS-7 cells
40. ER quality control: The cytoplasmic connection
41. Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products
42. Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes
43. Structure of the VHL-elongin C-elongin B complex: Implications for VHL tumor suppressor function