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

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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 PKCε to the plasma membrane.

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