Fig. 5: Bmal1 and Myh9 Interaction Increases MRTF-SRF Activity and Drives Cell State Change.
From: Cell state dependent effects of Bmal1 on melanoma immunity and tumorigenicity
a Upper panel: Diagram illustrating the interaction between Myh9, Actin and MRTF-SRF signal pathway. Myh9 (Myosin IIA) formed bipolar filaments binding to F-actin which can depolymerize into monomer G-actin. G-actin can bind to SRF cofactor MRTF to inhibit MRTF-SRF transcriptional activity. Lower panel: the diagram of SRF-RE Luciferase reporter to examine the activity of MRTF-SRF pathway. Created with BioRender.com. b, c Flow cytometry analysis of G-actin stained with Alexa594-conjugated DNaseI in YUMM2.1 EV, YUMM2.1 WT-Bmal1 and YUMM2.1 dHLH-Bmal1 cells. Data (b) represents 4 independent experiments which were quantified in (c). Data was normalized to EV. Mean ± SEM. Adjust p-value by one-way ANOVA test followed by multiple comparison test. d Relative luminescence (RLU) from YUMM2.1 EV, WT-Bmal1 and dHLH-Bmal1 cells that were transiently transfected with SRF-RE luciferase and Renilla luciferase plasmids and followed by treatment with 10 nM Trametinib (MEKi) for 20 h or 2 µM Cytochalasin D (CD) for 2 h. DMSO was the 20 h treatment control. Mean ± SEM of 6 BR. RE of 4. Adjust p-value by one-way ANOVA test followed by multiple comparisons test. ****p < 0.0001. BR biological replicate, RE replicate experiment. Source data are provided as a Source Data file.
