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 language | English |
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Pages (from-to) | 3501-3506 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 585 |
Issue number | 22 |
DOIs | |
Publication status | Published - 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