Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
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Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.9809826
We now identify SARA ( for Smad anchor for receptor activation ) , a FYVE domain protein that interacts directly with Smad 2 and Smad 3 . 0.9809826^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.90820461
Molecular modelling , supported by mutational analyses of Smad 2 and the SIM and the demonstration that the SARA SBD competes directly with the SIM for binding to Smad 2 , indicates that the SIM binds Smad 2 in the same hydrophobic pocket as does the proline rich rigid coil region of the SARA SBD . 0.90820461^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.86315273
Using co immunoprecipitation studies , we show that endogenous Smad 2 interacts with SARA after TGF beta 1 stimulation . 0.86315273^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Recently , Smad anchor for receptor activation ( SARA ) has been identified as a Smad 2 binding protein . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
The nuclear import function of Smad 2 is masked by SARA and unmasked by TGFbeta dependent phosphorylation . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Endofin also does not associate with Smad 2 nor behave like SARA in affecting transforming growth factor beta signaling . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
The linker protein SARA , which is required for Smad 2 signaling , disappears with transdifferentiation . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Structural basis of Smad 2 recognition by the Smad anchor for receptor activation . ^^^ The Smad anchor for receptor activation ( SARA ) recruits Smad 2 to the TGFbeta receptors for phosphorylation . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
We demonstrated that Hgs , a FYVE domain protein , binds to Smad 2 in its C terminal half and cooperates with another FYVE domain protein , the Smad anchor for receptor activation ( SARA ) , to stimulate activin receptor mediated signaling through efficient recruitment of Smad 2 to the receptor . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
All cells expressed components of the TGF beta / Smad signaling pathway including TGF beta 1 , T beta RI , T beta RII , Smad 2 , 3 , 4 , and Smad anchor for receptor activation . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Given that the signaling facilitating molecules Smad anchor for receptor activation ( SARA ) and Hrs are mainly localized in early endosomes , it was unclear whether receptor internalization is required for Smad 2 activation . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Our data provide evidence that , whereas type 1 receptor phosphorylation and association of SARA and Smad 2 with the TGF beta R complex take place independently of clathrin lattice formation , Smad 2 or Smad 3 activation and downstream signaling only occur after endocytic vesicle formation . ^^^
Interacting proteins: O95405 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 . ^^^ TGFbeta receptor mediated phosphorylation stimulates nuclear accumulation of Smad 2 by modifying its affinity for SARA and Smad 4 but not for CAN / Nup214 or Nup 153 . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Here we show that SARA localizes to endosomes containing EEA 1 , and that disruption of this localization inhibits TGF beta induced Smad 2 nuclear translocation . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Clathrin dependent internalization into the EEA 1 positive endosome , where the Smad 2 anchor SARA is enriched , promotes TGF beta signalling . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Additionally , SARA was found to modulate the self association of partially phosphorylated Smad 2 , which suggests an added role for this protein in preventing premature release of a monophosphorylated substrate from the receptor complex . ^^^
Interacting proteins: O95405 and Q15796 Pubmed SVM Score :0.0
Trx SARA bound specifically to Smad 2 and Smad 3 and inhibited both TGF beta induced reporter gene expression and epithelial to mesenchymal transition in NMuMG murine mammary epithelial cells . ^^^ In contrast to Smad 7 , Trx SARA had no effect on the Smad 2 or 3 phosphorylation levels induced by TGF beta 1 . ^^^ Trx SARA was primarily localized to the nucleus and perturbed the normal cytoplasmic localization of Smad 2 and 3 to a nuclear localization in the absence of TGF beta 1 , consistent with reduced Smad nuclear export . ^^^ The key mode of action of Trx SARA was to reduce the level of Smad 2 and Smad 3 in complex with Smad 4 after TGF beta 1 stimulation , a mechanism of action consistent with the preferential binding of SARA to monomeric Smad protein and Trx SARA mediated disruption of active Smad complexes . . ^^^