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. Author manuscript; available in PMC: 2018 Dec 21.
Published in final edited form as: Mol Cell. 2017 Dec 21;68(6):1067–1082.e12. doi: 10.1016/j.molcel.2017.11.026

Figure 6. AP-1 TFs interact with the BAF chromatin remodeling complex.

Figure 6

a) Summary of total peptides identified from Fos-EGFP or control immunoprecipitates analyzed by mass spectrometry. Additional information including Fold Change (FC) calculations are reported in Table S2. b) Western blots with indicated antibodies of anti-FLAG immunoprecipitates from stimulated (90m) wild-type (WT) or Fos-FlagHA knock-in MEFs. c–d) Western blots of input (left column) and proteins co-immunoprecipitated with FlagHA-tagged AP-1 family members (c) and indicated mutants of Fos (d) co-transfected with untagged Jun into HEK293T cells. Fos-basic mutant=specific amino acids mutated in the basic domain that binds DNA; Fos Δ–basic domain=basic domain complete deletion; FosL(1–5) mutant=all leucines in the leucine zipper mutated to valines (the leucine zipper is required for heterodimerization with Jun family proteins and thus for DNA binding); Fos Δ LZ =leucine zipper deletion. Transfected Fos family members exhibited variable expression levels, so, when possible, the amount of transfected plasmid was titrated to achieve similar expression levels (see methods). However, deletion of the entire basic domain in Fos (Fos Δ–basic domain) also destabilizes Jun protein, leading to reduced Jun levels and complicating our assessment of the effect of this deletion on AP-1’s ability to interact with BAF components.