Abstract

Phosphorylation of cytoskeletal proteins regulates the dynamics of polymerization, stability, and disassembly of the different types of cytoskeletal polymers. These control the ability of cells to migrate and divide. Mutations and alterations of the expression levels of multiple protein kinases are hallmarks of most forms of cancer. Thus, altered phosphorylation of cytoskeletal proteins is observed in most cancer cells. These alterations potentially control the ability of cancer cells to divide, invade and form distal metastasis. This review highlights the emergent role of phosphorylation in the control of the function of the different cytoskeletal polymers in cancer cells. It also addresses the potential effect of targeted inhibitors in the normalization of cytoskeletal function.

Highlights

  • Cytoskeletal proteins form the backbone of the different types of structural polymers found in every eukaryotic cell

  • We describe only the current state of the art regarding the phosphorylation of selected isoforms of actin, myosin II, tubulin and vimentin

  • We focus on the functional effect of these phosphorylations, and what the consequences would be if the extent of these phosphorylations was altered in the context of cancer progression

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Summary

Introduction

Cytoskeletal proteins form the backbone of the different types of structural polymers found in every eukaryotic cell. The effect of this phosphorylation in the regulation of the actin cytoskeleton in cancer cells has yet to be addressed, it could be related to its ability to polymerize and/or form filaments. Ser39 phosphorylation by protein kinase B (AKT/PKB) protects vimentin from proteolysis and enhances tumor growth and metastasis [69] by altering filament assembly [63], which regulates cortex plasticity and could underlie the fact that cancer cells are overall softer than non-cancer cells [70].

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