Protein kinase Cδ binds TIRAP/Mal to participate in TLR signaling

被引：42

作者：

Kubo-Murai, Miho

Hazeki, Kaoru ^{[1
]}

Sukenobu, Naoe

Yoshikawa, Kyoko

Nigorikawa, Kiyomi

Inoue, Kazumi

Yamamoto, Toshiyoshi

Matsumoto, Misako

Seya, Tsukasa

Inoue, Norimitsu

Hazeki, Osamu

机构：

[1] Hiroshima Univ, Grad Sch Biomed Sci, Div Mol Med Sci, Minami Ku, Hiroshima 7348551, Japan

[2] Kobe Univ, Biosignal Res Ctr, Kobe, Hyogo 6578501, Japan

[3] Hokkaido Univ, Grad Sch Med, Dept Microbiol & Immunol, Kita Ku, Sapporo, Hokkaido 0608638, Japan

[4] Osaka Med Ctr Canc & Cardiovasc Dis, Dept Immunol, Higashinari Ku, Osaka 5378511, Japan

来源：

MOLECULAR IMMUNOLOGY | 2007年 / 44卷 / 09期

关键词：

PKC delta; TLR; macrophage; signal transduction;

D O I：

10.1016/j.molimm.2006.11.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Toll-like receptor (TLR) family members recognize specific molecular patterns within pathogens. Signaling through TLRs results in a proximal event that involves direct binding of adaptor proteins to the receptors. We observed that TIRAP/Mal, an adaptor protein for TLR2 and TLR4, binds protein kinase C delta (PKC delta). TIRAP/Mal GST-fusion protein and a TIRAP/Mal antibody were able to precipitate PKC delta from rat peritoneal macrophage and THP1 cell lysates. Truncation mutants of TIRAP/Mal showed that the TIR domain of TIRAP/Mal is responsible for binding. TLR2- and TLR4-mediated phosphorylation of p38 MAPK, IKK, and IKB in RAW264.7 cells were abolished by depletion of PKC delta. These results suggest that PKC delta binding to TIRAP/Mal promotes TLR signaling events. (c) 2006 Elsevier Ltd. All rights reserved.

引用

页码：2257 / 2264

页数：8

共 43 条

[11] Toll-like receptor-mediated tyrosine phosphorylation of paxillin via MyD88-dependent and -independent pathways [J].