Protein kinase Cδ binds TIRAP/Mal to participate in TLR signaling
MolImmunol_44-9_2257.pdf 1.42 MB
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 Cδ (PKCδ). TIRAP/Mal GST-fusion protein and a TIRAP/Mal antibody were able to precipitate PKCδ 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 IκB in RAW264.7 cells were abolished by depletion of PKCδ. These results suggest that PKCδ binding to TIRAP/Mal promotes TLR signaling events.
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Pergamon-Elsevier Science Ltd.
Copyright (c) 2006 Elsevier Ltd
Graduate School of Biomedical Science