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Files in this Data Supplement:
Fig. S1. Alignment of different B subunits. Sequences for the B subunits α, β, δ, and γ were retrieved from the NCBI database and aligned using ClustalW. The alignment was edited using ESPRIPT. Peptides found by mass spectrometry in the proteomic screen for interaction partners of BMPRII are boxed.
Fig. S2. PP2A dephosphorylates BMP2-mediated C-terminally and linker-phosphorylated Smad1 in vitro. After BMP2 treatment, overexpressed Smad1 and Smad1 mutants were immunoprecipitated and subjected to in vitro dephosphorylation using recombinant PP2A. The precipitates were analyzed by SDS-PAGE and immunoblotting with anti-p-C-terminal and anti-P-linker antibody. Anti-Smad1 immunoblotting monitors the amount of Smad1 in each sample. The graph shows the C-terminal (grey) and the linker (black) phosphorylation of Smad1 and Smad1 mutants relative to their respective control (−BMP2, −PP2A). The intensities of the phospho-signals and the Smad1 signals of a representative experiment were measured with ImageJ.
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