Fig. 5: Phosphorylation and acetylation of KIF15 is opposite to PI3K-C2α interaction and FA depolymerization. | Cell Death & Disease

Fig. 5: Phosphorylation and acetylation of KIF15 is opposite to PI3K-C2α interaction and FA depolymerization.

From: Dynamic regulation of KIF15 phosphorylation and acetylation promotes focal adhesions disassembly in pancreatic cancer

Fig. 5

A Schematic model demonstrated the conservation analysis of the acetylation and phosphorylation of KIF15 in various species. B Capture-Elisa assay analysis of the integrin β1 recycling content in acetylation of K1009 inactivating or activating mutant of KIF15, S1169 and P1142 inactivating and activating mutant. C The effect of acetylation of K1009 inactivating or activating mutant of KIF15, S1169, and P1142 inactivating and activating mutant on the integrin β1/FAK pathway activity in whole cell lysis by western blot. D Immunofluorescence analysis of the acetylation of K1009 inactivating or activating mutant of KIF15, S1169 inactivating and activating mutant on the depolymerization of focal adhesions in PANC-1 cell. E The effect of K1009 activating mutant of KIF15, S1169 activating mutant on the integrin β1/FAK pathway activity in whole cell lysis by western blot and the interaction of KIF15, Rab11A Integrin β1, PI3K-C2α by Flag or HA immunoprecipitation assay. F Western blot analysis of the effects of K1009 deacetylation mutant of KIF15, S1169 activating mutant on integrin β1/FAK signaling in the wild-type or inactive state of RAB11A. All data represent means ± SEM; ***P < 0.001, **P < 0.01; *P < 0.05; two-tailed Student’s t test.

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