Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel - Lindau protein

Nature Cell Biology

Volumn 2, Issue 7, 2000, Pages 423-427

  Ohh, Michael ^a   Park, Cheol Won ^a,b   Ivan, Mircea ^a   Hoffman, Michael A ^a   Kim, Tae You ^a,b   Huang, L Eric ^a   Pavletich, Nikola ^b,c   Chau, Vincent ^d   Kaelin, William G ^a,b  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^d PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; F BOX PROTEIN; HYPOXIA INDUCIBLE FACTOR 1; UBIQUITIN; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

ARTICLE; CARCINOGENESIS; FAMILIAL CANCER; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROCESSING; VASCULAR TUMOR; VON HIPPEL LINDAU DISEASE;

CELL EXTRACTS; DEFEROXAMINE; DNA-BINDING PROTEINS; HELA CELLS; HUMANS; HYPOXIA-INDUCIBLE FACTOR 1; HYPOXIA-INDUCIBLE FACTOR 1, ALPHA SUBUNIT; LIGASES; MUTATION; NUCLEAR PROTEINS; OXYGEN; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, TERTIARY; PROTEINS; TRANSCRIPTION FACTORS; TRANSFECTION; TUMOR CELLS, CULTURED; TUMOR SUPPRESSOR PROTEINS; UBIQUITIN-PROTEIN LIGASES; UBIQUITINS; VON HIPPEL-LINDAU TUMOR SUPPRESSOR PROTEIN;

EID: 0033776536     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/35017054     Document Type: Article

References (20)

1. Structure of the VHL-elonginC-elonginB complex: Implications for VHL tumor suppressor function
2. Cancer. Many vessels, faulty gene
3. The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity
4. Identification of the von Hippel-Lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex
5. The von Hippel-Lindau gene product is necessary for oxgyen-dependent proteolysis of hypoxia-inducible factor α subunits
6. Regulation of hypoxia-inducible factor I alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway
7. Regulation of the hypoxia-inducible transcription factor 1 alpha by the ubiquitin-proteasome pathway
8. Activation of hypoxia-inducible factor-1: Definition of regulatory domains within the alpha subunit
9. The von Hippel-Lindau tumour suppressor protein: New perspectives
10. 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
11. Inhibition of transcriptional elongation by the VHL tumor suppressor protein
12. Binding of the von Hippel-Lindau tumor suppressor protein to elongin B and C
13. Hypoxia-inducible factor I alpha (HIF- 1 alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
14. Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein
15. Stabilization of wild-type p53 by hypoxia-inducible factor 1 alpha
16. Mitochondrial reactive oxygen species trigger hypoxia-induced transcription
17. Isolated familial pheochromocytoma as a variant of von Hippel-Lindau Disease
18. Identification of intragenic mutations in the von Hippel-Lindau disease tumor suppressor gene and correlation with disease phenotype
19. Tumor suppression by the human von Hippel-Lindau gene product
20. Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau protein requires binding to complexes containing elongins B/C and Cul2