Abstract 2166: Analyses of protein expression of PI 3-kinase/AKT signaling in response to altered expression of motor protein MYO1C

In this study, we assessed protein levels of 12 members of PI3-kinase/AKT signaling pathways in transient transfected HeLa cells expressing increasing amounts of MYO1C using Western blotting and densitometry analyses. Results revealed decreased protein levels of PTEN, AKT, and phosphorylated AKT, at both residues T308 and S473, and an increased expression of p110α protein in the cells transfected with the MYO1C gene expression constructs compared to the control cells transfected with empty plasmid. We next investigated potential effect of MYO1C protein depletion on serum-induced activation (phosphorylation) of AKT in the MCF10A cells that has de novo expression of MYO1C protein. Following serum stimulation, AKT was rapidly phosphorylated in its residue S473 (pAKTS473) in the cells transfected with MYO1C-siRNA, but with significantly lesser extent in the control cells. Overall, a negative correlation between the protein expression of MYO1C and AKT expression/activation was suggested, signifying a role for MYO1C as a negative regulator of PI3-kinsase/AKT signaling pathway. This is in agreement with the initial hypothesis of involvement of MYO1C in tumorigenesis pathways through its potential tumor suppressor activity. Further studies are required to fully understand the functional contribution of MYO1C to tumor development.Citation Format: Kittichate Visuttijai, Katarina Ejeskär, Afrouz Behboudi. Analyses of protein expression of PI 3-kinase/AKT signaling in response to alter...
Source: Cancer Research - Category: Cancer & Oncology Authors: Tags: Molecular and Cellular Biology Source Type: research