Fig. 4: TAK-981 treatment induces stronger binding of the cBAF complex to chromatin.

A Immunoblot of SS cells for specific BAF components was performed following treatment with no drug and 100 nM of TAK-981 for 36 h and differential salt extraction (0–1000 mM NaCl). GAPDH was used as a cytoplasmic loading control. Protein band intensities were quantified using GeneTools software with background subtraction and normalized to the expression of the strongest band within each blot, for drawing conclusions regarding the shift of each BAF complex component (elution at lower or higher salt concentrations) and the chromatin affinity before and after TAK-981 treatment, independent of the change in its total expression levels. B, C, D The band densities of ARID1A, SMARCE1 and BAF47 for the three SS cell lines from (A) were graphed using the GraphPad Prism software. E Illustration depicting the stabilization of the cBAF complex and the gain in its chromatin affinity after blocking SUMOylation compared to ncBAF and PBAF complexes (created in BioRender. Floros, K. (2025)). The colors that were used for the names of the BAF complex components throughout all figures of the manuscript are as follows: For unique cBAF complex subunits (e.g., ARID1A) a blue color has been used. For unique PBAF complex subunits (e.g., PBRM1 or ARID2) a green color has been used. For unique ncBAF complex subunits (e.g., BRD9 or GLTSCR1) a red color has been used. For cBAF/PBAF complex subunits (e.g., SMARCE1 or BAF47) a purple color has been used.