Figure S1.
Selection of mesenchymal (C2C12, MEFsv40, REF52) and epithelial (EPH4) cell lines to study BMP2 receptor dynamics. (A and B) The ability of the cell lines to respond to soluble BMP2 stimulation was validated by the phosphorylation and nuclear translocation of SMAD 1/5 after 4 h of treatment by (A) immunoblotting and (B) immunofluorescence visualized by confocal microscopy. Quantification of nuclear P-Smad: N ≥ 100 cells per condition. Scale bar, 100 µm. (C) Immunoblots of opto-BMPRs and opto-β3 Integrin showing expression of the opto-proteins at the expected molecular weight. (D) Improvement of the visualization of transmembrane BMPR by total internal reflection microscopy (TIRFM) by examining a thin section of the sample at the adherent cell surface relative to confocal microscopy. Opto-β3 integrin is observed within the FA sites. Scale bar, 15 µm. Source data are available for this figure: SourceData FS1.

Selection of mesenchymal (C2C12, MEFsv40, REF52) and epithelial (EPH4) cell lines to study BMP2 receptor dynamics. (A and B) The ability of the cell lines to respond to soluble BMP2 stimulation was validated by the phosphorylation and nuclear translocation of SMAD 1/5 after 4 h of treatment by (A) immunoblotting and (B) immunofluorescence visualized by confocal microscopy. Quantification of nuclear P-Smad: N ≥ 100 cells per condition. Scale bar, 100 µm. (C) Immunoblots of opto-BMPRs and opto-β3 Integrin showing expression of the opto-proteins at the expected molecular weight. (D) Improvement of the visualization of transmembrane BMPR by total internal reflection microscopy (TIRFM) by examining a thin section of the sample at the adherent cell surface relative to confocal microscopy. Opto-β3 integrin is observed within the FA sites. Scale bar, 15 µm. Source data are available for this figure: SourceData FS1.

This Feature Is Available To Subscribers Only

or Create an Account

Close Modal
Close Modal