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

Authors
Wei, Jun-DongKim, Joo-YoungKim, Jae-Hong
Issue Date
16-11월-2011
Publisher
ELSEVIER SCIENCE BV
Keywords
Leukotriene B-4 receptor 2 (BLT2); Chemotaxis; Akt; Reactive oxygen species
Citation
FEBS LETTERS, v.585, no.22, pp.3501 - 3506
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
585
Number
22
Start Page
3501
End Page
3506
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/111139
DOI
10.1016/j.febslet.2011.10.037
ISSN
0014-5793
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.
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생명과학대학 (생명과학부)
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