BLT2 phosphorylation at Thr(355) by Akt is necessary for BLT2-mediated chemotaxis

Abstract

BLT2, a low-affinity leukotriene B-4 (LTB4) receptor, is a member of the G protein-coupled receptor family and is involved in multiple cellular responses, including chemotaxis. Despite its biological significance, the mechanisms of BLT2 regulation, especially by protein kinases, are poorly characterised. In this study, we found that Akt phosphorylates BLT2 at its C-terminal Thr(355) residue and that this event is critical for BLT2-mediated chemotactic responses. In addition, we found that Rac1 stimulation and subsequent reactive oxygen species (ROS) production lie downstream of BLT2 phosphorylation, thus mediating chemotaxis. Structured summary of protein interactions: BLT2 physically interacts with Akt by pull down (View interaction) BLT2 physically interacts with Akt by pull down (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.