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Binding Dynamics of Smad3 and cPML: Insights from TGF-β1 Signaling Pathways

This study investigates the interactions between Smad3 and cPML in the context of TGF-β1 signaling. Using a series of co-immunoprecipitation experiments, we explore the binding affinities of various Smad3 constructs along with different segments of the cPML protein. The findings highlight the significance of the MH1 and MH2 domains in mediating these interactions, which are crucial for understanding the molecular mechanisms of TGF-β1 signaling in cellular responses. This research contributes to the broader knowledge of Smad protein functionality in transcriptional regulation.

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Binding Dynamics of Smad3 and cPML: Insights from TGF-β1 Signaling Pathways

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  1. Supp. Fig.3 c a Smad3 cPML binding Smad3 binding cPML MH1 Linker MH2 R B1-B2 C-C C-terminal + + 1 425 1 MH1 Linker + B1-B2 C-C C-terminal + 1 270 98 - Linker MH2 _ C-C C-terminal 425 170 228 475 MH2 - 270 425 b d Input IP:PML IP: Xpress Smad3 Smad3 WB: Flag Smad3 1-270 WB:Xpress Smad3 170-425 cPML WB: Xpress cPML 98-475 Smad3 270-425 cPML 228-475 cPML WB:PML Flag-Smad3 Input - - Xpress-Smad3 + - + - - + - + - - Flag-Smad3 - + + + + Xpress-Smad3 170-425 - - - - - - - - - - + + Xpress-cPML - + + - - - - Xpress-Smad3 270-425 - - - + - - - - + - Xpress-cPML 98-475 - - - + - - - Xpress-Smad3 1-270 - - - - + - - - - + Xpress-cPML 228-475 - - - - + cPML - + + + + - + + + + + + TGF-1 - - + - -

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