Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 52, Pages 36166-36178Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.612630
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Funding
- Wellcome Trust [08667/Z/08/Z]
- Friends of Anchor Trust [BM114 RGB4561]
- University of Aberdeen
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Formyl-peptide receptor type 2 (FPR2; also called ALX because it is the receptor for lipoxin A(4)) sustains a variety of biological responses relevant to the development and control of inflammation, yet the cellular regulation of this G-protein-coupled receptor remains unexplored. Here we report that, in response to peptide agonist activation, FPR2/ALX undergoes beta-arrestin-mediated endocytosis followed by rapid recycling to the plasma membrane. We identify a transplantable recycling sequence that is both necessary and sufficient for efficient receptor recycling. Furthermore, removal of this C-terminal recycling sequence alters the endocytic fate of FPR2/ALX and evokes pro-apoptotic effects in response to agonist activation. This study demonstrates the importance of endocytic recycling in the anti-apoptotic properties of FPR2/ALX and identifies the molecular determinant required for modulation of this process fundamental for the control of inflammation.
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