| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Hypoxic conditions lead to the formation of a DNA binding complex containing both HIF 1 alpha and p300 / CBP . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Redox regulated recruitment of the transcriptional coactivators CREB binding protein and SRC 1 to hypoxia inducible factor 1alpha . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Structural basis for recruitment of CBP / p300 by hypoxia inducible factor 1 alpha . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Physiology meets biophysics : visualizing the interaction of hypoxia inducible factor 1 alpha with p 300 and CBP . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Structural basis for Hif 1 alpha / CBP recognition in the cellular hypoxic response . ^^^ Under hypoxic conditions , HIF 1 activates transcription of critical adaptive genes by recruitment of the general coactivators CBP / p300 through interactions with its alpha subunit ( Hif 1 alpha ) . ^^^ To delineate the structural basis for this interaction , we have determined the solution structure of the complex between the carboxy terminal activation domain ( CAD ) of Hif 1 alpha and the zinc binding TAZ 1 ( CH 1 ) motif of cyclic AMP response element binding protein ( CREB ) binding protein ( CBP ) . ^^^ The structure of this complex provides new insights into the mechanism through which Hif 1 alpha recruits CBP / p300 in response to hypoxia . . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| In the context of full length HIF 1 alpha , mutation of the leucine residues conferred conformational changes to the protein and significantly reduced the transactivation function as well as functional interaction with the transcriptional coactivators CBP and SRC 1 . ^^^ These mutations also affected intranuclear redistribution of HIF 1 alpha in the presence of CBP , indicating that the integrity of the C TAD is critical for intracellular localization of mouse HIF 1 alpha . . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The transactivation activity of HIF complexes requires the recruitment of p300 / CREB binding protein ( CBP ) by HIF 1 alpha and HIF 2 alpha that undergo oxygen dependent degradation . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Signal transduction in hypoxic cells : inducible nuclear translocation and recruitment of the CBP / p300 coactivator by the hypoxia inducible factor 1alpha . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The CH 1 domain of CBP / p300 was considered essential for most , if not all , hypoxia inducible transcription by binding to hypoxia inducible factor 1alpha ( HIF 1alpha ) . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| P35srj interferes with the recruitment of p300 / CBP by the transcription factor HIF 1alpha , a process that is essential for the transcriptional response to hypoxia . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Cited 2 is a cAMP responsive element binding protein ( CBP ) / p300 interacting transcriptional modulator and a proposed negative regulator for hypoxia inducible factor ( HIF ) 1alpha through its competitive binding with HIF 1alpha to CBP / p300 . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Third , the association of HIF 1alpha with von Hippel Lindau was decreased but the association with CREB binding protein was enhanced in the presence of HBx , suggesting the molecular mechanism by which HBx enhances the protein stability and transactivation function of HIF 1alpha . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The TAZ 1 domain of the homologous transcriptional coactivators CREB binding protein ( CBP ) and p 300 forms a complex with CITED 2 ( CBP / p300 interacting transactivator with ED rich tail ) , inhibiting the activity of the hypoxia inducible factor ( HIF 1alpha ) and thereby attenuating the cellular response to low tissue oxygen concentration . ^^^ The HIF 1alpha and CITED 2 domains utilize partly overlapping surfaces of TAZ 1 to achieve high affinity binding and to compete effectively with each other for interaction with CBP / p300 ; CITED 2 and HIF 1alpha use these binding sites differently to maintain similar binding affinities in order to displace each other in a feedback loop during the hypoxic response . . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The activity of HIF 1alpha is regulated by binding to the transcriptional co activator cAMP response element binding protein binding protein ( CBP ) / p300 . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| Further , the carboxy terminus of HBx enhanced the transactivation function of HIF 1alpha by enhancing its association with CREB binding protein ( CBP ) . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| We have previously shown that HIF 1alpha and the transcriptional coactivator CBP colocalize in accumulation foci within the nucleus of hypoxic cells . ^^^ Biochemical assays showed that depletion of CBP from cell extracts abrogated interaction between SRC 1 and HIF 1alpha . ^^^ Thus , in contrast to the current model for the assembly of complexes between nuclear hormone receptors and coactivators , the present data suggest that it is CBP that recruits SRC 1 to HIF 1alpha in hypoxic cells . ^^^ We also observed that CBP , HIF 1alpha / Arnt and HIF 1alpha / CBP accumulation foci partially overlap with the hyperphosphorylated form of RNA polymerase 2 , and that CBP had a stabilizing effect on the formation of the complex between HIF 1alpha and its DNA binding partner , Arnt . ^^^ In conclusion , CBP plays an important role as a mediator of HIF 1alpha / Arnt / CBP / SRC 1 complex formation , coordinating the temporally and hierarchically regulated intranuclear traffic of HIF 1alpha and associated cofactors in signal transduction in hypoxic cells . . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The C terminal activation domain ( C TAD ) of the hypoxia inducible transcription factors HIF 1alpha and HIF 2alpha binds the CH 1 domains of the related transcriptional coactivators CREB binding protein ( CBP ) and p 300 , an oxygen regulated interaction thought to be highly essential for hypoxia responsive transcription . ^^^ |
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| Interacting proteins: Q16665 and Q92793 |
Pubmed |
SVM Score :0.0 |
| The hydroxyproline then interacts with ubiquitin E 3 ligase , the von Hippel Lindau protein , leading to degradation of HIF 1alpha by ubiquitin dependent proteasomes , while the hydroxylation of the asparagine residue prevents recruitment of the coactivator , cAMP response element binding protein ( CBP ) , thereby decreasing the transactivation ability of HIF 1alpha . ^^^ In hypoxic cells , TPEN also prevents HIF 1alpha from interacting with CBP , so reducing expression of HIF 1alpha target genes . ^^^ |
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