Fig. 8.

LncLrrc55-AS promotes the interaction between PME-1 and PP2A. a RNA FISH-immunofluorescence detection of endogenous lncLrrc55-AS, PME-1, and PP2A-C in peritoneal macrophages from WT or lncLrrc55-AS^−/− non-infected mice and mice infected with SeV for 12 h. Scale bars, 10 µm. b Quantitative analysis of colocalization rate for PME-1 and PP2A in NC- or lncLrrc55-AS-silenced peritoneal macrophages after SeV infection for 12 h. c Interaction between PME-1 and PP2A in RAW264.1 cells. NC- or lncLrrc55-AS-silenced cells were infected with VSV for the indicated hours, followed by immunoprecipitation with anti-PME-1 antibody. The immunoprecipitated PME-1 and PP2A were detected by western blot. d Interaction between PME-1 and PP2A in WT and lncLrrc55-AS^−/− peritoneal macrophages infected with SeV for the indicated hours. Samples isolated from cells were equally divided into three parts. All parts were digested with Rnase A or Rnase T1 (10 U/mL), followed by immunoprecipitation with anti-PME-1 antibody (two parts) or with normal IgG antibody (one part; control). The immunoprecipitated PME-1 and PP2A were detected by western blot. e Interactions of PME-1 and PP2A with lncLrrc55-AS in an overexpression system. HEK293T cells were transfected with plasmids encoding PME-1-Flag, PP2A-C-Myc, and lncLrrc55-AS, followed by immunoprecipitation with anti-Flag antibody-coupled beads. The immunoprecipitated PME-1-Flag and PP2A-C-Myc were detected by western blot analysis. HEK293T cells transfected with empty vector plasmids were used as controls. Data are from three independent experiments (b, means ± SEM) or are representative of three independent experiments with similar results (a, c–e). *P < 0.05 (Student’s t-test)