Eps8 controls actin-based motility by capping the barbed ends of actin filaments

Andrea Disanza, Marie France Carlier, Theresia E B Stradal, Dominique Didry, Emanuela Frittoli, Stefano Confalonieri, Assunta Croce, Jurgen Wehland, Pier Paolo Di Fiore, Giorgio Scita

Research output: Contribution to journalArticlepeer-review


Actin filament barbed-end capping proteins are essential for cell motility, as they regulate the growth of actin filaments to generate propulsive force. One family of capping proteins, whose prototype is gelsolin, shares modular architecture, mechanism of action, and regulation through signalling-dependent mechanisms, such as Ca2+ or phosphatidylinositol-4,5-phosphate binding. Here we show that proteins of another family, the Eps8 family, also show barbed-end capping activity, which resides in their conserved carboxy-terminal effector domain. The isolated effector domain of Eps8 caps barbed ends with an affinity in the nanomolar range. Conversely, full-length Eps8 is auto-inhibited in vitro, and interaction with the Abi1 protein relieves this inhibition. In vivo, Eps8 is recruited to actin dynamic sites, and its removal impairs actin-based propulsion. Eps8-family proteins do not show any similarity to gelsolin-like proteins. Thus, our results identify a new family of actin cappers, and unveil novel modalities of regulation of capping through protein-protein interactions. One established function of the Eps8-Abi1 complex is to participate in the activation of the small GTPase Rac, suggesting a multifaceted role for this complex in actin dynamics, possibly through the participation in alternative larger complexes.

Original languageEnglish
Pages (from-to)1180-1188
Number of pages9
JournalNature Cell Biology
Issue number12
Publication statusPublished - Dec 2004

ASJC Scopus subject areas

  • Cell Biology


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