Capping protein regulators fine-tune actin assembly dynamics

Marc Edwards, Adam Zwolak, Dorothy A. Schafer, David Sept, Roberto Dominguez, John A. Cooper

Research output: Contribution to journalReview articlepeer-review

111 Scopus citations

Abstract

Capping protein (CP) binds the fast growing barbed end of the actin filament and regulates actin assembly by blocking the addition and loss of actin subunits. Recent studies provide new insights into how CP and barbed-end capping are regulated. Filament elongation factors, such as formins and ENA/VASP (enabled/vasodilator-stimulated phosphoprotein), indirectly regulate CP by competing with CP for binding to the barbed end, whereas other molecules, including V-1 and phospholipids, directly bind to CP and sterically block its interaction with the filament. In addition, a diverse and unrelated group of proteins interact with CP through a conserved 'capping protein interaction' (CPI) motif. These proteins, including CARMIL (capping protein, ARP2/3 and myosin I linker), CD2AP (CD2-associated protein) and the WASH (WASP and SCAR homologue) complex subunit FAM21, recruit CP to specific subcellular locations and modulate its actin-capping activity via allosteric effects.

Original languageEnglish
Pages (from-to)677-689
Number of pages13
JournalNature Reviews Molecular Cell Biology
Volume15
Issue number10
DOIs
StatePublished - Jan 1 2014

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