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

  • bioRxiv. 2026 Jun 1:2026.05.28.728515. doi: 10.64898/2026.05.28.728515.
M Kathryn Malone  1 Christopher W Brownlee  1  2
Affiliations
  • 1. Department of Pharmacological Sciences, Stony Brook University; Stony Brook, 11794, United States of America.
  • 2. Lead Contact.
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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