Src-dependent phosphorylation of Scar1 promotes its association with the Arp2/3 complex

Hazel Ardern, Emma Sandilands, Laura M Machesky, Paul Timpson, Margaret C Frame, Valerie G Brunton

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The WAVE/Scar proteins regulate actin polymerisation at the leading edge of motile cells via activation of the Arp2/3 complex in response to extracellular cues. Within cells they form part of a pentameric complex that is thought to regulate their ability to interact and activate the Arp2/3 complex. However, the exact mechanism for this is not known. We set out to assess whether phosphorylation of Scar1 by the non-receptor tyrosine kinase Src may influence the function of Scar1 and its ability to regulate Arp2/3-mediated actin polymerisation. We show that Scar1 is phosphorylated by Src in vitro and in vivo and identify tyrosine 125 as the major site in Scar1 to be phosphorylated in cells. Src-dependent phosphorylation of Scar1 on tyrosine 125 enhances its ability to bind to the Arp2/3 complex and regulates its ability to control actin polymerisation in cells. Thus, Src may act as an intermediary to regulate the activity of the Arp2/3 complex in response to external stimuli, via modulation of its interaction with WAVE/Scar proteins.
Original languageEnglish
Pages (from-to)6-13
Number of pages8
JournalCell motility and the cytoskeleton
Issue number1
Publication statusPublished - Jan 2006

Keywords / Materials (for Non-textual outputs)

  • Actin-Related Protein 2-3 Complex
  • Actins
  • Animals
  • COS Cells
  • Cercopithecus aethiops
  • Phosphorylation
  • Stress Fibers
  • Transfection
  • Wiskott-Aldrich Syndrome Protein Family
  • src-Family Kinases


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