Palmitoylated importin α recruits PKCε to the plasma membrane to drive breast cancer cell motility

Abstract

Importin is a nuclear transport factor which canonically has a role in binding and shuttling NLS-containing proteins from the cytoplasm into the nucleus. Recently, it has been shown that when palmitoylated by specific palmitoyl acyl transferases, importin can partition to the plasma membrane where its roles remain widely unknown. Patients with breast cancer displaying increased importin expression have advanced tumor size, poor tumor differentiation, and reduced overall and recurrence-free survival. In this study, we use palmitoylation altering pharmacological agents to demonstrate that membrane bound palmitoylated importin enhances breast cancer cell motility through binding and tethering the serine/threonine kinase PKC{varepsilon} to the plasma membrane.