Fig. 5

The protein-protein interaction between Gαh and PLC-δ1 regulates the invasive ability of TNBC cells and serves as a poor prognostic marker in breast cancer patients. a A schematic representation for the construction of the PLC-δ1-binding site deletion mutant of the Gαh protein. b and c Giemsa staining b and quantification (c) of the invaded H1806 cells after 16 h of transfection with empty vector (VC) or plasmid expressing wild-type (wt) or deletion-mutant (Δ657-687) Gαh. In c, different letters above the columns indicate significant differences between the means (p < 0.05). d Demonstration of the synthesis of the myristoylated (Myr) PLC-δ1 peptide. e and f e Giemsa staining and f quantification of invaded MDA-MB-231 cells treated with non-Myr (control, CTL, and orange column) or Myr-PLC-δ1 (blue column) peptide at the designated concentrations for 16 h. g IHC staining for Gαh and PLC-δ1 with their specific antibodies in breast cancer tissues. h Kaplan-Meier analysis of the Gαh/PLC-δ1 signature and the probability of DFS in breast cancer patients. i Correlation of PLC-δ1 or the Gαh/PLC-δ1 signature with lymph node metastasis in ER-negative breast cancer. In c and f, the data from three independent experiments were presented as the mean ± SEM