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CUTTING EDGE |
B-Activating Kinase-Associated Protein 1 Participates in TLR3/Toll-IL-1 Homology Domain-Containing Adapter Molecule-1-Mediated IFN Regulatory Factor 3 Activation1
Departments of
*
Immunology and
Molecular Biology, Osaka Medical Center for Cancer and Cardiovascular Diseases, Osaka, Japan;
Division of Molecular Biology, Nara Institute for Science and Technology, Nara, Japan;
Department of Biochemistry and Cell Biology, Graduate School of Medicine, Nagoya City University, Nagoya, Japan; and
¶ Department of Microbiology and Immunology, Graduate School of Medicine, Hokkaido University, Sapporo, Japan
TLRs signal the presence of microbial patterns and activate transcription factors. In TLR3 and TLR4, the adapter Toll-IL-1R homology domain-containing adapter molecule (TICAM-1) (also called Toll/IL-1R domain-containing adapter inducing IFN-
(TRIF)) mediates IFN regulatory factor 3 (IRF3) phosphorylation followed by IFN- production. The regulatory subunit TNFR-associated factor family member-associated NF-
B activator (TANK) couples with the kinase complex IB kinase-related kinase 
/NF-B-activating kinase (NAK) (TANK-binding kinase 1 (TBK1)) that involveTICAM-1-dependent IFN- induction. There are several TANK-homologous proteins. We tested whether TICAM-1 binds and coprecipitates with TANK or its family proteins. The results are: 1) the TANK family protein NAK-associated protein 1 (NAP1), but not TANK, coprecipitates withTICAM-1; 2) NAP1 overexpression markedly enhances TBK1-mediated IFN- promoter activation; 3) a dominant-negative form, NAP (158–270), suppresses IRF3 activation in response to poly(I:C) or LPS; 4) RNA interference targeting of the NAP1 message results in a failure of poly(I:C)-mediated IRF3 polymerization and IFN- production. Thus, NAP1 is the kinase subunit responsible for TLR3/4-mediated IFN- induction in the TICAM-1 pathway.
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