Hypoxia-inducible factor-1α (HIF-1 escapes O2-driven proteasomal degradation irrespective of its subcellular localization: Nucleus or cytoplasm

EMBO Reports

Volumn 2, Issue 7, 2001, Pages 615-620

  Berra, E ^a   Roux, D ^a   Richard, D E ^a   Pouyssegur J ^a  

^a CENTRE DE BIOCHIMIE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

HELIX LOOP HELIX PROTEIN; HYPOXIA INDUCIBLE FACTOR 1; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 1BETA; LEPTOMYCIN B; OXYGEN; PROTEASOME; PROTEIN MDM2; PROTEIN P53; PROTON; SODIUM ION; UNCLASSIFIED DRUG;

ARTICLE; CELL COMPARTMENTALIZATION; CELL HYPOXIA; CELL NUCLEUS; CONTROLLED STUDY; CYTOPLASM; ENZYME DEGRADATION; ENZYME LOCALIZATION; EUKARYOTE; GENE CONTROL; HALF LIFE TIME; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTON SODIUM EXCHANGE;

ACETYLCYSTEINE; ACTIVE TRANSPORT, CELL NUCLEUS; ANTIBIOTICS, ANTINEOPLASTIC; CELL FRACTIONATION; CELL HYPOXIA; CELL LINE; CELL NUCLEUS; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; CYTOPLASM; FATTY ACIDS, UNSATURATED; HUMANS; IMMUNOBLOTTING; MULTIENZYME COMPLEXES; OXYGEN; PROTEASOME ENDOPEPTIDASE COMPLEX; RECOMBINANT FUSION PROTEINS; SODIUM-HYDROGEN ANTIPORTER; TRANSCRIPTION FACTORS; TRANSFECTION;

EUKARYOTA;

EID: 0034904751     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kve130     Document Type: Article

References (27)

1. HIF-1-dependent transcriptional activity is required for oxygen-mediated HIF-1α degradation
2. Induction and nuclear translocation of hypoxia-inducible factor-1 (HIF-1): Heterodimerization with ARNT is not necessary for nuclear accumulation of HIF-1α
3. Hypoxia inducible factor-α binding and ubiquitylation by the von Hippel-Lindau tumor suppressor protein
4. + exchangers
5. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
6. CRM1 is an export receptor for leucine-rich nuclear export signals
7. Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
8. Identification of alternative spliced variants of human hypoxia-inducible factor-1α
9. The hypoxic response: Huffing and HIFing
10. Cloning of a factor required for activity of the Ah (dioxin) receptor
11. 2-dependent degradation domain via the ubiquitin-proteasome pathway
12. 2 sensing
13. 2-regulated prolyl hydroxylation
14. Signal transduction in hypoxic cells: Inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1α
15. Regulation of the hypoxia-inducible transcription factor 1α by the ubiquitin-proteasome pathway
16. The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis
17. Ubiquitination of hypoxia-inducible factor requires direct binding to the β-domain of the von Hippel-Lindau protein
18. Evidence for a role of CRM1 in signal-mediated nuclear protein export
19. Gene transfer in vascular cells using an engineered Na-H exchanger (NHE1) as a selectable marker
20. Regulation of tumor angiogenesis by p53-induced degradation of hypoxia-inducible factor 1α
21. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor-1α (HIF-1α) and enhance the transcriptional activity of HIF-1
22. Nonhypoxic pathway mediates the induction of hypoxia-inducible factor 1α in vascular smooth muscle cells
23. Hypoxia-inducible factor 1α (HIF-1α) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
24. + antiporter
25. 2 homeostasis
26. Mechanism of regulation of the hypoxia-inducible factor-1α by the von Hippel-Lindau tumor suppressor protein
27. Purification and characterization of hypoxia-inducible factor 1