Skip to main content
. Author manuscript; available in PMC: 2018 Jan 1.
Published in final edited form as: Cancer Res. 2016 Nov 7;77(1):187–197. doi: 10.1158/0008-5472.CAN-16-1267-T

Figure 5. PCDH7 represses PP2A by facilitating inhibitory interactions with SET.

Figure 5

A, Western blot analysis of FLAG-tagged SET immunoprecipitates in HBEC-shp53 cells. B, Reciprocal co-immunoprecipitation of endogenous PCDH7 and SET in KRAS mutant H1944 cells. C, Reciprocal co-immunoprecipitation of endogenous PCDH7 and PP2A-A or PP2A-C in KRAS mutant H1944 cells. D, Western blot analysis of FLAG-tagged SET immunoprecipitates in HBEC-shp53-KRASG12V and HBEC-shp53-KRASG12V-PCDH7 cells. E, Quantification of PP2A activity in HBEC-shp53-KRASG12V cells with overexpression of PCDH7 and knockout of SET. F, Western blot showing reduced phospho-ERK1/2 in clonal SET knockout HBEC-shp53-KRASG12V-PCDH7 cells and rescued phospho-ERK1/2 levels upon expression of a mutant SET-β cDNA that is resistant to Cas9 cleavage (Lenti-SET-CR). G, Quantification of soft agar assays demonstrating that SET is required for PCDH7-induced transformation of HBEC-shp53-KRASG12V cells. H, Western blot demonstrating that FTY720 treatment reduced ERK activation in HBEC-shp53-KRASG12V-PCDH7 cells. I, Western blot analysis demonstrating a dose-dependent effect of FTY720 on phospho-ERK in HBEC-shp53-KRASG12V-PCDH7 cells. J, Western blot showing increased ERK activation in HBEC-shp53-KRASG12V-PCDH7 cells treated with Okadaic Acid for 75 min. A longer exposure is shown to highlight the baseline level of phospho-ERK1/2 in untreated cells.