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

Lookup NU author(s): Professor Paul RaceORCiD


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

Publication metadata

Author(s): Tilley FC, Williamson RC, Race PR, Rendall TC, Bass MD

Publication type: Article

Publication status: Published

Journal: Small GTPases

Year: 2015

Volume: 6

Issue: 1

Pages: 36-42

Online publication date: 10/04/2015

Acceptance date: 24/11/2014

ISSN (print): 2154-1248

ISSN (electronic): 2154-1256

Publisher: Landes Bioscience


DOI: 10.4161/21541248.2014.992259

PubMed id: 25862165


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