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 |
|---|---|
| Pages (from-to) | 3501-3506 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 585 |
| Issue number | 22 |
| DOIs | |
| Publication status | Published - 2011 Nov 16 |
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Keywords
- Akt
- Chemotaxis
- Leukotriene B receptor 2 (BLT2)
- Reactive oxygen species
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology
Cite this
BLT2 phosphorylation at Thr355 by Akt is necessary for BLT2-mediated chemotaxis. / Wei, Jun Dong; Kim, Joo Young; Kim, Jae-Hong.
In: FEBS Letters, Vol. 585, No. 22, 16.11.2011, p. 3501-3506.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - BLT2 phosphorylation at Thr355 by Akt is necessary for BLT2-mediated chemotaxis
AU - Wei, Jun Dong
AU - Kim, Joo Young
AU - Kim, Jae-Hong
PY - 2011/11/16
Y1 - 2011/11/16
N2 - 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).
AB - 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).
KW - Akt
KW - Chemotaxis
KW - Leukotriene B receptor 2 (BLT2)
KW - Reactive oxygen species
UR - http://www.scopus.com/inward/record.url?scp=80855131521&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80855131521&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2011.10.037
DO - 10.1016/j.febslet.2011.10.037
M3 - Article
C2 - 22044535
AN - SCOPUS:80855131521
VL - 585
SP - 3501
EP - 3506
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 22
ER -