Fig. 4 |. The differential ability of TAZ and YAP to undergo phase separation lies in the CC domain.

a, Domain structure of TAZ chimaeras. b, Coomassie blue staining of various recombinant proteins purified from Escherichia coli. c, Droplet formation by TAZ chimaeras using the same conditions as described in Fig. 3a. Scale bar, 10 μm. Quantification of the droplets is shown on the right. Data are mean ± s.e.m. Statistical significance was evaluated using one-way ANOVA with Krusk–Wallis test. Droplets in n = 3 fields in each group were quantified. d, Confocal microscopy images of MCF-10A cells transfected with various chimaeras as indicated. Scale bar, 10 μm. Insets, magnified by 2.94, 2.94, 2.94 and 3.12 times, respectively. right, quantification of the percentage of cells that displayed nuclear puncta. Data are mean ± s.e.m. P values were determined using unpaired two-tailed Student’s t-tests; 80 transfected cells in each group were quantified; n = 3 biologically independent samples. e, Flag-tagged WT TAZ or YAP was cotransfected into HEK293T cells together with HA-tagged TAZ mutants or YAP as indicated. Dimerization of TAZ or YAp was evaluated using immunoprecipitation with anti-Flag antibodies and detected using western blotting with anti-HA antibodies (top). The abundance of these proteins in the cell lysates was assessed using western blotting (bottom). GApDH was used as a loading control. The experiments in b–e were repeated independently three times with similar results. Source data are available online.