The Role Of Shoc2 In Regulating Cell Motility

The extracellular‐signal‐regulated kinase 1/2 (ERK1/2) signaling cascade is a fundamental cellular process that orchestrates diverse biological outcomes including cell growth, proliferation, migration, and apoptosis. Mutations of the components in ERK1/2 signaling pathway are often found in cancer cells and tumors. ERK1/2 activity is controlled by scaffold proteins that assemble unique signaling complexes, target multi‐protein signaling modules to certain cellular locations and enhance the activity of ERK1/2 substrates at particular sub‐cellular localizations. Thus, scaffolds deliver signal specificity and determine the biological outputs of the ERK1/2 pathway. Ras‐Raf‐binding scaffold protein, Shoc2, is essential for proper ERK1/2 pathway signaling upon epidermal growth factor receptor (EGFR) activation. Decrease in Shoc2 levels leads to significant reduction in ERK1/2 phosphorylation upon EGF treatment. Here we focus on studying physiological role of ERK1/2 signals transmitted through Shoc2 module. We observed that cells with Shoc2 depleted using lentivirus‐delivered shRNA have higher rates of cell proliferation. We also see that the depletion of Shoc2 results in dramatic decrease in cell migration and adhesion. All together, these results suggest that Shoc2 has an important role in regulating cell motility and may contribute to cancer/tumor development.