| Interacting proteins: P51692 and Q9Y618 |
Pubmed |
SVM Score :0.0 |
| Functional interaction of STAT 5 and nuclear receptor co repressor SMRT : implications in negative regulation of STAT 5 dependent transcription . ^^^ In a search for STAT 5 interacting proteins by yeast two hybrid screening , we identified the nuclear receptor co repressor SMRT ( silencing mediator for retinoic acid receptor and thyroid hormone receptor ) as a potential STAT 5 binding partner . ^^^ SMRT binds to both STAT5A and 5B , and strongly repressed STAT 5 dependent transcription in vitro . ^^^ SMRT binds to the N terminal coiled coil domain of STAT 5 and a mutation within this region previously found to render STAT 5 hyperactive in response to cytokines abolished the interaction with SMRT . ^^^ Overexpression of SMRT suppressed the induction of STAT 5 target genes by interleukin 3 , whereas the histone deacetylase inhibitor trichostatin A effectively enhanced and prolonged their expression . ^^^ |
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| Interacting proteins: P51692 and Q9Y618 |
Pubmed |
SVM Score :0.0 |
| To determine the molecular mechanisms of myeloid leukemogenesis and maturation arrest in STAT5b RARalpha ( + ) APL and its unresponsiveness to ATRA , we examined the effect of STAT5b RARalpha on the activity of myeloid transcription factors including RARalpha / retinoid 10 receptor ( RXR ) alpha , STAT 3 , and STAT 5 as well as its molecular interactions with the nuclear receptor corepressor , SMRT , and nuclear receptor coactivator , TRAM 1 . ^^^ |
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| Interacting proteins: P51692 and Q9Y618 |
Pubmed |
SVM Score :0.0 |
| Oligomerization of this domain in the Stat 5 RARalpha fusion protein leads to stable binding of the corepressor SMRT independent of all trans retinoic acid ( ATRA ) stimulation and is accompanied by an impaired response to differentiation signals in hematopoietic cells . ^^^ |
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