| Interacting proteins: P42226 and Q15788 |
Pubmed |
SVM Score :0.0 |
| Transcriptional activation by STAT 6 requires the direct interaction with NCoA 1 . ^^^ We found that only one of them , NCoA 1 , acts as a coactivator for STAT 6 and interacts directly with the transactivation domain of STAT 6 . ^^^ The N terminal part of NCoA 1 interacts with the far C terminal part of the STAT 6 transactivation domain but does not interact with the other members of the STAT family . ^^^ This domain of NCoA 1 has a strong inhibitory effect on STAT 6 mediated transactivation when overexpressed in cells , illustrating the importance of NCoA 1 for STAT 6 mediated transactivation . ^^^ In addition , we showed that both coactivators CBP and NCoA 1 bind independently to specific regions within the STAT 6 transactivation domain . ^^^ |
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| Interacting proteins: P42226 and Q15788 |
Pubmed |
SVM Score :0.0 |
| An LXXLL motif in the transactivation domain of STAT 6 mediates recruitment of NCoA 1 / SRC 1 . ^^^ The CREB binding protein and the nuclear coactivator 1 ( NCoA 1 ) , a member of the p160 / steroid receptor coactivator family , bind independently to specific regions of STAT 6 and act as coactivators . ^^^ In this study we show that an LXXLL motif in the STAT 6 transactivation domain mediates the interaction with NCoA 1 . ^^^ Taken together , these results indicate that the STAT 6 LXXLL binding motif mediates the interaction with NCoA 1 in transcriptional activation and represents a new potential drug target for the inhibition of the STAT 6 transactivation function in allergic diseases . . ^^^ |
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| Interacting proteins: P42226 and Q15788 |
Pubmed |
SVM Score :0.0 |
| The p 160 coactivator nuclear coactivator 1 ( Src 1 ) was specifically recruited by and coactivated Stat 6 but not the chimeric Stat 6 molecules . ^^^ |
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| Interacting proteins: P42226 and Q15788 |
Pubmed |
SVM Score :0.0 |
| Structure of the NCoA 1 / SRC 1 PAS B domain bound to the LXXLL motif of the STAT 6 transactivation domain . ^^^ The CREB binding protein ( p300 / CBP ) and the nuclear coactivator 1 ( NCoA 1 ) , a member of the p160 / steroid receptor coactivator family , bind independently to specific regions of the STAT 6 transactivation domain and act as coactivators . ^^^ The interaction between STAT 6 and NCoA 1 is mediated by an LXXLL motif in the transactivation domain of STAT 6 . ^^^ To define the mechanism of coactivator recognition , we determined the crystal structure of the NCoA 1 PAS B domain in complex with the STAT 6 LXXLL motif . ^^^ The amphipathic , alpha helical STAT 6 LXXLL motif binds mostly through specific hydrophobic interactions to NCoA 1 . ^^^ |
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| Interacting proteins: P42226 and Q15788 |
Pubmed |
SVM Score :0.0 |
| The staphylococcal nuclease like ( SN ) domains of p 100 directly interacted with amino acids 1099 1758 of CBP , while p 100 did not associate with SRC 1 , another coactivator of STAT 6 . p 100 was found to recruit histone acetyltransferase ( HAT ) activity to STAT 6 in vivo . ^^^ |
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