BLT2 phosphorylation at Thr355 by Akt is necessary for BLT2-mediated chemotaxis

FEBS Lett. 2011 Nov 16;585(22):3501-6. doi: 10.1016/j.febslet.2011.10.037. Epub 2011 Oct 29.

Abstract

BLT2, a low-affinity leukotriene B(4) (LTB(4)) 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CHO Cells
  • Chemotaxis*
  • Cricetinae
  • Humans
  • Phosphorylation
  • Proto-Oncogene Proteins c-akt / metabolism*
  • Reactive Oxygen Species / metabolism
  • Receptors, Leukotriene B4 / genetics
  • Receptors, Leukotriene B4 / metabolism*
  • Signal Transduction
  • Threonine / genetics*
  • Threonine / metabolism
  • rac1 GTP-Binding Protein / metabolism

Substances

  • LTB4R2 protein, human
  • Reactive Oxygen Species
  • Receptors, Leukotriene B4
  • Threonine
  • Proto-Oncogene Proteins c-akt
  • rac1 GTP-Binding Protein