Fig. 5: PDE4DIP promotes NF1 degradation through activation of PKCε. | Cell Death & Disease

Fig. 5: PDE4DIP promotes NF1 degradation through activation of PKCε.

From: PDE4DIP contributes to colorectal cancer growth and chemoresistance through modulation of the NF1/RAS signaling axis

Fig. 5: PDE4DIP promotes NF1 degradation through activation of PKCε.The alternative text for this image may have been generated using AI.

A Immunofluorescence staining showing the subcellular localization of NF1 in control (siNC) and PDE4DIP-silenced (siP1) CRC cells. Scale bar, 10 μm. B Western blot analysis was performed to determine the cytoplasmic and nuclear NF1 levels in control (siNC) and PDE4DIP-silenced (siP1) CRC cells. C Western blot analysis of the MARCKS and phosphorylated MARCKS (pMARCKS) levels in control (siNC) and PDE4DIP-silenced (siP1, siP2) CRC cells. D Western blot analysis of the total PKCε, phosphorylated PKCε (pPKCε) and phosphorylated pan-PKC (pPKC) levels in control and PDE4DIP-silenced CRC cells. E Western blot analysis of the activation of PKC in PDE4DIP-overexpressing CRC cells. DLD1 and SW480 cells were transfected with empty vector (Vec) or the Myc-tagged PDE4DIP expression plasmid (PI) for 48 h. F Western blot showing that the PKCε inhibitor EV1-2 blocked the PDE4DIP-promoted reduction in NF1 and phosphorylation of ERK. Cells transfected with empty vector (Vec) or the PDE4DIP expression plasmid (PI) were exposed to DMSO or EV1-2 (1.0 μM) for 30 min.

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