Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.60017308
FAST 2 also interacts directly with Smad 2 , a cytoplasmic protein which is translocated to the nucleus in response to TGF beta , and forms a multimeric complex with Smad 2 and Smad 4 on the activin response element , a high affinity binding site for FAST 1 . 0.60017308^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :1.0436627
Although significantly different in sequence from its Xenopus counterpart , hFAST 1 shared with xFAST 1 the ability to bind to human Smad 2 and activate an activin response element ( ARE ) . 1.0436627^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.92026114
Using two point mutations of Smad 2 previously identified in colorectal carcinomas , we show that Smad 2 ushers Smad 4 to the nucleus to form a transcriptional activation complex with the nuclear DNA binding protein FAST 1 and that the mutant proteins interact normally with FAST 1 but fail to recruit Smad 4 into the nucleus . 0.92026114^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.73870264
FAST 1 has been shown to associate with Smad 2 and Smad 4 , transducers of TGFbeta superfamily signals , in response to stimulation by several TGFbeta superfamily ligands . 0.73870264^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.86529065
These results and the association of FoxH 1 and Mixer / Bon with phosphorylated Smad 2 support a role for these factors as components of the Nodal signaling pathway . 0.86529065^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Smad 2 and Smad 3 positively and negatively regulate TGF beta dependent transcription through the forkhead DNA binding protein FAST 2 . ^^^ FAST 2 binds to a sequence in the gsc promoter , but efficient transcriptional activation and assembly of a DNA binding complex of FAST 2 , Smad 2 , and Smad 4 requires an adjacent Smad 4 site . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
However , Smad 3 behaves differently from Smad 2 in regulating transcription by a winged helix transcription factor , FAST 2 , on an activin responsive element ( ARE ) in the Xenopus Mix . 2 promoter . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
This motif is not confined to these homeodomain proteins , but is also present in the Smad 2 interacting winged helix proteins Xenopus Fast 1 , human Fast 1 , and mouse Fast 2 . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Structural basis for the functional difference between Smad 2 and Smad 3 in FAST 2 ( forkhead activin signal transducer 2 ) mediated transcription . ^^^ In FAST 2 ( forkhead activin signal transducer 2 ) mediated transcriptional regulation using the activin responsive element derived from Xenopus Mix . 2 promoter as a reporter , Smad 3 but not Smad 2 alone was able to stimulate the transcription . ^^^ Taken together , these results suggest that , as compared with Smad 2 , the unique function of Smad 3 in modulating the FAST 2 mediated transcription is contributed to by a subtle difference in the structural features at the MH 1 domain . . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Furthermore , the interaction of FAST 2 with BF 1 is mediated by the same domain which is required for FAST 2 to interact with Smad 2 . ^^^ We propose a model in which BF 1 interferes with transcriptional responses to TGF beta by interacting with FAST 2 or with other DNA binding proteins which function as Smad 2 partners and which have a common mode of interaction with Smad2 . . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
After TGF beta mediated phosphorylation and association with Smad 4 , Smad 2 moves to the nucleus and activates expression of specific genes through cooperative interactions with DNA binding proteins , including members of the winged helix family of transcription factors , forkhead activin signal transducer ( FAST ) 1 and FAST 2 . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
In transient transfection experiments , overexpression of CBF Cb was able to repress the transactivating activity of Smad 2 and Smad 3 , mediated either by direct binding to the Smad responsive element or through their association with the Smad interacting transcription factor FAST 2 ( forkhead activin signal transducer 2 ) . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
The winged helix transcription factor forkhead activin signal transducer 1 ( Fast 1 ) acts as a co factor for Smad 2 [ 12 20 ] . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
We now report that Smad 4 is present in ARF , and that FAST 1 , Smad 4 and Smad 2 co immunoprecipitate in a ligand regulated fashion . ^^^ In a yeast two hybrid assay , the FAST 1 carboxy terminus interacts with Smad 2 but not Smad 4 . ^^^ Deletion mutants of the FAST 1 carboxy terminus that still participate in ligand regulated Smad 2 binding no longer associated with Smad 4 or ARF . ^^^ These results indicate that Smad 4 stabilizes a ligand stimulated Smad 2 FAST 1 complex as an active DNA binding factor . . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Smad 4 is not required for nuclear translocation of Smads 1 or 2 , or for association of Smad 2 with a DNA binding partner , the winged helix protein FAST 1 . ^^^ Receptor activated Smad 2 takes Smad 4 into the nucleus where they form a complex with FAST 1 that requires these three components to activate transcription . ^^^ Smad 4 contributes two functions : Through its amino terminal domain , Smad 4 promotes binding of the Smad2 / Smad4 / FAST 1 complex to DNA ; through its carboxy terminal domain , Smad 4 provides an activation function required for Smad 1 or Smad 2 to stimulate transcription . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
In contrast , Smad 2 ( wt ) , Smad2Deltaexon3 , and Smad 3 efficiently formed ARE binding complexes with Smad 4 and FAST 1 , although Smad 2 ( wt ) did not directly bind to ARE . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Furthermore , association between Smads and FAST 1 , a mediator of mesoderm induction by activin , is dependent upon the presence of the Smad 2 C1 sequence . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
This complex contains Smad 2 or Smad 3 , Smad 4 , and a novel forkhead transcription factor , FAST 1 , and binds to an enhancer ( activin responsive element ; ARE ) that confers activin regulation of Mix . 2 transcription . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Smad 4 HL2 did not induce the activation of pAR 3 Lux , which contains FAST 1 binding sites and is activated by a complex composed of FAST 1 , Smad 2 and Smad 4 . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
All these Smad 4 variants form complexes with activated Smad 2 and Smad 3 and are incorporated into DNA binding complexes with the transcription factor Fast 1 , regardless of the amount of linker they contain . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Transforming growth factor beta ( TGF beta ) / activin induced Smad2 / Smad4 complexes are recruited to different promoter elements by transcription factors , such as Fast 1 or the Mix family proteins Mixer and Milk , through a direct interaction between Smad 2 and a common Smad interaction motif ( SIM ) in the transcription factors . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
CAN / Nup214 and Nup 153 compete with the cytoplasmic retention factor SARA and the nuclear Smad 2 partner FAST 1 for binding to a hydrophobic corridor on the MH 2 surface of Smad 2 . ^^^
Interacting proteins: O75593 and Q15796 Pubmed SVM Score :0.0
Moreover , ELAC 2 was shown to specifically associate with the nuclear Smad 2 partner , FAST 1 and to potentiate the interaction of activated Smad 2 with transcription factor Sp 1 . ^^^