Iintegration of the Rac1- and actin-binding properties of coronin-1C

Frances C. Tilley, Rosalind C. Williamson, Paul R. Race, Thomas C. Rendall, Mark D. Bass*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

8 Citations (Scopus)


The coronin family of actin-binding proteins regulate actin branching by inhibiting Arp2/3. We recently reported 2 interactions that were unique to coronin-1C: binding of a Rac1 inhibitor, RCC2, to the unique linker region and Rac1 itself to the propeller domain in a manner that differs from that proposed for other coronins. Through these interactions coronin-1C redistributes Rac1 from the back of the cell to the leading edge for either activation or sequestration by the associated Rac1-inhibitor, RCC2. Here we investigate the relationship between the Rac1- and actinbinding properties of coronin-1C and find that, although actin appears to be involved in the retrafficking of Rac1, signaling by Rac1 lies upstream of the stress fiber-formation, for which the coronins were originally characterized.

Original languageEnglish
Pages (from-to)36-42
Number of pages7
JournalSmall GTPases
Issue number1
Publication statusPublished - 10 Apr 2015


  • Actin
  • Coronin-1C
  • Endocytosis
  • Rac1
  • Trafficking


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