Sci. Signal., 30 April 2013
Arresting Chemokine ScavengingChemokines 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).
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