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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.
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
URL: https://doi.org/10.4161/21541248.2014.992259
DOI: 10.4161/21541248.2014.992259
PubMed id: 25862165
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