Western blotting was performed according to standard methods as previously described (14 (link)). Cells and tissues were lysed with radioimmunoprecipitation assay lysis buffer (Biyuntian Biotechnology Research Institute, Nantong, China). The protein concentration of each lysate was determined with the BCA Protein Assay kit (Thermo Fisher Scientific, Inc.). Total proteins (30 µg/lane) were separated by 10% SDS-PAGE and transferred to a polyvinylidene difluoride (PVDF) membrane. The blots were blocked in 5% milk for 1 h at room temperature. PVDF membranes were incubated using rabbit anti-LASP2 (1:100; cat. no. 260630; Sigma-Aldrich; Merck KGaA, Darmstadt, Germany), anti-cyclin D1 (1:10,000; cat. no. ab134175; Abcam, Cambridge, UK) and anti-β-catenin (1:1,000; cat. no. ab22656; Abcam) antibodies overnight at 4°C. Subsequently, membranes were incubated with corresponding horseradish peroxidase-conjugated goat anti-rabbit secondary antibodies (1:5,000; cat. no. ab6112; Abcam) for 2 h at room temperature and detected using an enhanced chemiluminescence reagent (ECL Prime; GE Healthcare, Chicago, IL, USA). The anti-α-tubulin (1:5,000; cat. no. ab4074; Abcam,) and anti-P84 (1:10,000; cat. no. ab131268; Abcam) antibodies were used as loading controls.