Literature DB >> 17161867

Protein kinase Cdelta binds TIRAP/Mal to participate in TLR signaling.

Miho Kubo-Murai1, Kaoru Hazeki, Naoe Sukenobu, Kyoko Yoshikawa, Kiyomi Nigorikawa, Kazumi Inoue, Toshiyoshi Yamamoto, Misako Matsumoto, Tsukasa Seya, Norimitsu Inoue, Osamu Hazeki.   

Abstract

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 Cdelta (PKCdelta). TIRAP/Mal GST-fusion protein and a TIRAP/Mal antibody were able to precipitate PKCdelta 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 IkappaB in RAW264.7 cells were abolished by depletion of PKCdelta. These results suggest that PKCdelta binding to TIRAP/Mal promotes TLR signaling events.

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Year:  2006        PMID： 17161867     DOI： 10.1016/j.molimm.2006.11.005

Source DB:  PubMed          Journal:  Mol Immunol        ISSN： 0161-5890            Impact factor:   4.407


  22 in total

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