Fascin promotes filopodia formation independent of its role in actin bundling

Research output: Contribution to journalArticle

  • External authors:
  • Jennifer Zanet
  • Asier Jayo
  • Serge Plaza
  • Maddy Parsons
  • Brian Stramer

Abstract

Fascin is an evolutionarily conserved actin-binding protein that plays a key role in forming filopodia. It is widely thought that this function involves fascin directly bundling actin filaments, which is controlled by an N-terminal regulatory serine residue. In this paper, by studying cellular processes in Drosophila melanogaster that require fascin activity, we identify a regulatory residue within the C-terminal region of the protein (S289). Unexpectedly, although mutation (S289A) of this residue disrupted the actin-bundling capacity of fascin, fascin S289A fully rescued filopodia formation in fascin mutant flies. Live imaging of migrating macrophages in vivo revealed that this mutation restricted the localization of fascin to the distal ends of filopodia. The corresponding mutation of human fascin (S274) similarly affected its interaction with actin and altered filopodia dynamics within carcinoma cells. These data reveal an evolutionarily conserved role for this regulatory region and unveil a function for fascin, uncoupled from actin bundling, at the distal end of filopodia. © 2012 Zanet et al.

Bibliographical metadata

Original languageEnglish
Pages (from-to)477-486
Number of pages9
JournalJournal of Cell Biology
Volume197
Issue number4
DOIs
Publication statusPublished - May 2012