The cofilin activity cycle in lamellipodia and invadopodia

Matthew Oser, John Condeelis

Research output: Contribution to journalReview article

126 Scopus citations

Abstract

The actin severing protein cofilin is essential for directed cell migration and chemotaxis, in many cell types and is also important for tumor cell invasion during metastasis. Through its severing activity, cofilin increases the number of free barbed ends to initiate actin polymerization for actin-based protrusion in two distinct subcellular compartments in invasive tumor cells: lamellipodia and invadopodia. Cofilin severing activity is tightly regulated and multiple mechanisms are utilized to regulate cofilin activity. In this prospect, we have grouped the primary on/off regulation into two broad categories, both of which are important for inhibiting cofilin from binding to F-actin or G-actin: (1) Blocking cofilin activity by the binding of cofilin to either PI(4,5)P2 at lamellipodia, or cortactin at invadopodia. (2) Blocking cofilin's ability to bind to actin via serine phosphorylation. Although the literature suggests that these cofilin regulatory mechanisms may be cell-type dependent, we propose the existence of a common cofilin activity cycle in which both operate. In this common cycle, the mechanism used to initiate cofilin activity is determined by the starting point in the cycle in a given subcellular compartment.

Original languageEnglish (US)
Pages (from-to)1252-1262
Number of pages11
JournalJournal of Cellular Biochemistry
Volume108
Issue number6
DOIs
StatePublished - Dec 15 2009

Keywords

  • Actin polymerization
  • Arp2/3 complex
  • Chemotaxis
  • PIP2
  • cortactin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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