Cofilin takes the lead

Research output: Contribution to journalArticle

226 Citations (Scopus)

Abstract

Cofilin has emerged as a key regulator of actin dynamics at the leading edge of motile cells. Through its actin-severing activity, it creates new actin barbed ends for polymerization and also depolymerizes old actin filaments. Its function is tightly regulated in the cell. Spatially, its activity is restricted by other actin-binding proteins, such as tropomyosin, which compete for accessibility of actin filament populations in different regions of the cell. At the molecular level, it is regulated by phosphorylation, pH and phosphatidylinositol (4,5)-bisphosphate binding downstream of signaling cascades. In addition, it also appears to be regulated by interactions with 14-3-3ζ and cyclase-associated protein. In vivo, cofilin acts synergistically with the Arp2/3 complex to amplify local actin polymerization responses upon cell stimulation, which gives it a central role in setting the direction of motility in crawling cells.

Original languageEnglish (US)
Pages (from-to)19-26
Number of pages8
JournalJournal of Cell Science
Volume118
Issue number1
DOIs
StatePublished - Jan 1 2005

Fingerprint

Actin Depolymerizing Factors
Actins
Actin Cytoskeleton
Polymerization
Actin-Related Protein 2-3 Complex
Microfilament Proteins
Tropomyosin
Phosphatidylinositols
Phosphorylation
Lead
Population
Proteins

Keywords

  • Arp2/3 complex
  • Chemotaxis
  • Stimulated protrusion model

ASJC Scopus subject areas

  • Cell Biology

Cite this

Cofilin takes the lead. / Desmarais, Vera M.; Ghosh, Mousumi; Eddy, Robert J.; Condeelis, John S.

In: Journal of Cell Science, Vol. 118, No. 1, 01.01.2005, p. 19-26.

Research output: Contribution to journalArticle

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