Fig. 7: ARHGAP4 enhances MYH9 phase separation and mediates the recruitment and assembly of GSK3β.

A Molecular dynamics analysis of the interaction strength between ARHGAP4 and MYH9; B The formation of MYH9 and ARHGAP4 aggregates in vivo when ARHGAP4 was overexpressed and not overexpressed, and the uptake was at a scale of 10 um; C The co-localization of MYH9 (GFP) and ARHGAP4 (mcherry) in vivo and the FRAP imaging of the co-formed aggregates were taken at a scale of 10 um; D In vivo and in vitro imaging uptake of the aggregates formed by ARHGAP4 and MYH9 before and after the addition of 1.6-hexanediol at a scale of 10 um; E MYH9 protein uptake in vivo and in vitro at a scale of 10 um; F The co-localization of MYH9 (GFP) and ARHGAP4 (mcherry) in vitro and the FRAP imaging of the co-formed aggregates were taken at a scale of 10 um; G the formation of MYH9 aggregates after different ARHGAP4 was transferred, and the uptake was at a scale of 10 um; H Co-IP analysis of GSK3β complex assembly in HCT116 cells and RKO cells transfected with PCDNA, ARHGAP4-WT and ARHGAP4-MUT plasmids after knockdown of ARHGAP4; I In vivo fluorescence analysis of the recruitment of GSK3β by MYH9 aggregates was taken at a scale of 10 um; J WB was used to detect the changes of β-catenin pathway after transfection of PCDNA, ARHGAP4-WT and ARHGAP4-MUT plasmids; K WB was used to detect the distribution of β-catenin in PCDNA, ARHGAP4-WT and ARHGAP4-MUT transfected cells.