pubmed-article:19880525 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1333336 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0215848 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0256079 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
pubmed-article:19880525 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:19880525 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:19880525 | pubmed:dateCreated | 2010-1-18 | lld:pubmed |
pubmed-article:19880525 | pubmed:abstractText | Activation of transcription in response to low oxygen tension is mediated by the hypoxia-inducible factor-1 (HIF-1). HIF-1 is a heterodimer of two proteins: aryl hydrocarbon receptor nuclear translocator and the oxygen-regulated HIF-1 alpha. The C-terminal activation domain of HIF-1 alpha has been shown to interact with cysteine/histidine-rich region 1 (CH1) of the coactivator CBP/p300 in a hypoxia-dependent manner. However, HIF forms lacking C-terminal activation domain (naturally occurring or genetically engineered) are still able to activate transcription of target genes in hypoxia. Here, we demonstrate that the N-terminal activation domain (N-TAD) of HIF-1 alpha interacts with endogenous CBP and that this interaction facilitates its transactivation function. Our results show that interaction of HIF-1 alpha N-TAD with CBP/p300 is mediated by the CH3 region of CBP known to interact with, among other factors, p53. Using fluorescence resonance energy transfer experiments, we demonstrate that N-TAD interacts with CH3 in vivo. Coimmunoprecipitation assays using endogenous proteins showed that immunoprecipitation of CBP in hypoxia results in the recovery of a larger fraction of HIF-1 alpha than of p53. Chromatin immunoprecipitation demonstrated that at 1% O(2) CBP is recruited to a HIF-1 alpha but not to a p53 target gene. Upon activation of both pathways, lower levels of chromatin-associated CBP were detected at either target gene promoter. These results identify CBP as the coactivator directly interacting with HIF-1 alpha N-TAD and mediating the transactivation function of this domain. Thus, we suggest that in hypoxia HIF-1 alpha is a major CBP-interacting transcription factor that may compete with other CBP-dependent factors, including p53, for limiting amounts of this coactivator, underscoring the complexity in the regulation of gene expression by HIF-1 alpha. | lld:pubmed |
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pubmed-article:19880525 | pubmed:language | eng | lld:pubmed |
pubmed-article:19880525 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:19880525 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:19880525 | pubmed:month | Jan | lld:pubmed |
pubmed-article:19880525 | pubmed:issn | 1083-351X | lld:pubmed |
pubmed-article:19880525 | pubmed:author | pubmed-author:RoederRobert... | lld:pubmed |
pubmed-article:19880525 | pubmed:author | pubmed-author:PoellingerLor... | lld:pubmed |