The role of palladin in actin organization and cell motility

Eur J Cell Biol. 2008 Sep;87(8-9):517-25. doi: 10.1016/j.ejcb.2008.01.010. Epub 2008 Mar 14.

Abstract

Palladin is a widely expressed protein found in stress fibers, focal adhesions, growth cones, Z-discs, and other actin-based subcellular structures. It belongs to a small gene family that includes the Z-disc proteins myopalladin and myotilin, all of which share similar Ig-like domains. Recent advances have shown that palladin shares with myotilin the ability to bind directly to F-actin, and to crosslink actin filaments into bundles, in vitro. Studies in a variety of cultured cells suggest that the actin-organizing activity of palladin plays a central role in promoting cell motility. Correlative evidence also supports this hypothesis, as palladin levels are typically up-regulated in cells that are actively migrating: in developing vertebrate embryos, in cells along a wound edge, and in metastatic cancer cells. Recently, a mutation in the human palladin gene was implicated in an unusually penetrant form of inherited pancreatic cancer, which has stimulated new ideas about the role of palladin in invasive cancer.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actin Cytoskeleton / physiology
  • Actin Cytoskeleton / ultrastructure*
  • Animals
  • Cell Adhesion Molecules / metabolism
  • Cell Movement / physiology*
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism
  • Cytoskeleton / metabolism
  • Humans
  • Microfilament Proteins / genetics
  • Microfilament Proteins / physiology*
  • Models, Biological
  • Mutation
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism
  • Transforming Growth Factor beta1 / metabolism
  • Wound Healing / physiology

Substances

  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • Microfilament Proteins
  • PALLD protein, human
  • Phosphoproteins
  • Transforming Growth Factor beta1