Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. Signal., 30 April 2013
Vol. 6, Issue 273, p. ra30
[DOI: 10.1126/scisignal.2003627]


Editor's Summary

Arresting Chemokine Scavenging
Chemokines are chemoattractant cytokines, gradients of which stimulate the directed migration of cells to target sites, for example, during inflammation or infection. Chemokines signal through conventional chemokine receptors, which are G protein–coupled receptors; however, chemokines also bind to a subset of receptors, the atypical chemokine receptors (ACRs), that have no known signaling function. Borroni et al. found that chemokine binding to D6, a prototypical ACR that acts as a scavenger to degrade chemokines, activated a β-arrestin–dependent, but G protein–independent, signaling pathway involving the actin-binding protein cofilin that was required for its functions. These findings suggest that D6 is a β-arrestin–biased signaling receptor and that this pathway is required for chemokine scavenging.

Citation: E. M. Borroni, C. Cancellieri, A. Vacchini, Y. Benureau, B. Lagane, F. Bachelerie, F. Arenzana-Seisdedos, K. Mizuno, A. Mantovani, R. Bonecchi, M. Locati, β-Arrestin–Dependent Activation of the Cofilin Pathway Is Required for the Scavenging Activity of the Atypical Chemokine Receptor D6. Sci. Signal. 6, ra30 (2013).

Read the Full Text

Science Signaling Podcast: 30 April 2013.
E. M. Borroni, R. Bonecchi, and A. M. VanHook (2013)
Science Signaling 6, pc11
   Abstract »    Full Text »

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882