http://purl.uniprot.org/citations/11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11454738 | http://www.w3.org/2000/01/rdf-schema#comment | "Eukaryotic cells sense oxygen and adapt to hypoxia by regulating a number of genes. Hypoxia-inducible factor 1 (HIF-1) is the 'master' in this pleiotypic response. HIF-1 comprises two members of the basic helix--loop--helix transcription factor family, HIF-1 alpha and HIF-1 beta. The HIF-1 alpha protein is subject to drastic O(2)-dependent proteasomal control. However, the signalling components regulating the 'switch' for 'escaping' proteasomal degradation under hypoxia are still largely unknown. The rapid nuclear translocation of HIF-1 alpha could represent an efficient way to escape from this degradation. We therefore asked, where in the cell is HIF-1 alpha degraded? To address this question, we trapped HIF-1 alpha either in the cytoplasm, by fusing HIF-1 alpha to the cytoplasmic domain of the Na(+)-H(+) exchanger (NHE-1), or in the nucleus, by treatment with leptomycin B. Surprisingly, we found that HIF-1 alpha is stabilized by hypoxia and undergoes O(2)-dependent proteasomal degradation with an identical half-life (5--8 min) in both cellular compartments. Therefore, HIF-1 alpha entry into the nucleus is not, as proposed, a key event that controls its stability. This result markedly contrasts with the mechanism that controls p53 degradation via MDM2."xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.org/dc/terms/identifier | "doi:10.1093/embo-reports/kve130"xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/author | "Pouyssegur J."xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/author | "Berra E."xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/author | "Roux D."xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/author | "Richard D.E."xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/name | "EMBO Rep"xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/pages | "615-620"xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/title | "Hypoxia-inducible factor-1 alpha (HIF-1 alpha) escapes O(2)-driven proteasomal degradation irrespective of its subcellular localization: nucleus or cytoplasm."xsd:string |
http://purl.uniprot.org/citations/11454738 | http://purl.uniprot.org/core/volume | "2"xsd:string |
http://purl.uniprot.org/citations/11454738 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11454738 |
http://purl.uniprot.org/citations/11454738 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11454738 |
http://purl.uniprot.org/uniprot/#_Q15008-mappedCitation-11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11454738 |
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http://purl.uniprot.org/uniprot/#_A6NIX2-mappedCitation-11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11454738 |
http://purl.uniprot.org/uniprot/#_O43242-mappedCitation-11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11454738 |
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http://purl.uniprot.org/uniprot/#_P62837-mappedCitation-11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11454738 |
http://purl.uniprot.org/uniprot/#_Q13200-mappedCitation-11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11454738 |
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http://purl.uniprot.org/uniprot/#_Q15369-mappedCitation-11454738 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/11454738 |