Cortactin: a multifunctional regulator of cellular invasiveness

Cell Adh Migr. Mar-Apr 2011;5(2):187-98. doi: 10.4161/cam.5.2.14773. Epub 2011 Mar 1.


Branched actin assembly is critical for a variety of cellular processes that underlie cell motility and invasion, including cellular protrusion formation and membrane trafficking. Activation of branched actin assembly occurs at various subcellular locations via site-specific activation of distinct WASp family proteins and the Arp2/3 complex. A key branched actin regulator that promotes cell motility and links signaling, cytoskeletal and membrane trafficking proteins is the Src kinase substrate and Arp2/3 binding protein cortactin. Due to its frequent overexpression in advanced, invasive cancers and its general role in regulating branched actin assembly at multiple cellular locations, cortactin has been the subject of intense study. Recent studies suggest that cortactin has a complex role in cellular migration and invasion, promoting both on-site actin polymerization and modulation of autocrine secretion. Diverse cellular activities may derive from the interaction of cortactin with site-specific binding partners.

Publication types

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

MeSH terms

  • Actin Cytoskeleton / physiology
  • Actin-Related Protein 2 / metabolism*
  • Actin-Related Protein 3 / metabolism*
  • Actins / metabolism*
  • Animals
  • Binding Sites
  • Biomarkers, Tumor / genetics
  • Biomarkers, Tumor / metabolism
  • Cell Communication
  • Cell Movement*
  • Cortactin* / genetics
  • Cortactin* / metabolism
  • Cytoskeleton / metabolism
  • Female
  • Gene Expression
  • Humans
  • Mice
  • Neoplasms / genetics
  • Neoplasms / metabolism
  • Polymerization
  • Protein Binding
  • Protein Structure, Tertiary
  • Signal Transduction
  • Wiskott-Aldrich Syndrome Protein Family / metabolism*


  • Actin-Related Protein 2
  • Actin-Related Protein 3
  • Actins
  • Biomarkers, Tumor
  • Cortactin
  • Wiskott-Aldrich Syndrome Protein Family