Reorganisation of the dendritic actin network during cancer cell migration and invasion

Semin Cancer Biol. 2008 Feb;18(1):12-22. doi: 10.1016/j.semcancer.2007.08.001. Epub 2007 Sep 4.


Invasion of cancer cells into surrounding tissues has a causal role in tumour progression and is an initial step in tumour metastasis. It requires cell migration, which is driven by the polymerisation of actin within two distinct structures, lamellipodia and filopodia, and attachment to the extracellular matrix through actin-rich adhesive structures. Podosomes and invadopodia are modified adhesive structures that not only establish contact with the substratum, but are also involved in matrix degradation leading to invasion. Actin dynamics and organisation are tightly regulated processes responsible for the range of different and specific cellular functions in response to various stimuli. This review explores the mechanistic basis of tumour cell invasion by focusing on the reorganisation of the dendritic actin network. Actin filaments are flexible structures that are poorly able to resist bending forces, causing them to bend rather than push when encountering obstacles. During migration, cells overcome this problem either by creating a dense array of short-branched filaments as found in lamellipodia, or by bundling filaments as found in filopodia. Here we discuss the possible switch mechanism for the two modes of actin organisation and the advantages of each in the perspective of cell migration and invasion during tumour metastasis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actin Cytoskeleton / physiology*
  • Actin Cytoskeleton / ultrastructure
  • Actins / chemistry
  • Actins / metabolism*
  • Animals
  • Cell Movement
  • Cytoskeleton / physiology*
  • Cytoskeleton / ultrastructure
  • Humans
  • Listeria / ultrastructure
  • Microfilament Proteins / metabolism
  • Neoplasm Invasiveness
  • Neoplasm Metastasis
  • Neoplasms / pathology*
  • Neoplasms / physiopathology*
  • Pseudopodia / physiology*
  • Pseudopodia / ultrastructure


  • Actins
  • Microfilament Proteins