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

Jun Dong Wei, Joo Young Kim, Jae Hong Kim

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

BLT2, a low-affinity leukotriene B4 (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 Thr355 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).

Original languageEnglish
Pages (from-to)3501-3506
Number of pages6
JournalFEBS Letters
Volume585
Issue number22
DOIs
Publication statusPublished - 2011 Nov 16

Keywords

  • Akt
  • Chemotaxis
  • Leukotriene B receptor 2 (BLT2)
  • Reactive oxygen species

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'BLT2 phosphorylation at Thr<sup>355</sup> by Akt is necessary for BLT2-mediated chemotaxis'. Together they form a unique fingerprint.

  • Cite this