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Trif-related adapter molecule is phosphorylated by protein kinase C epsilon during Toll-like receptor 4 signalling
MCGETTRICK-DILLON, ANNE; O'NEILL, LUKE ANTHONY JOHN; PALSSON, EVA
peer-reviewed PKC? has been shown to play a key role in the effect of the Gram-negative bacterial product LPS; however, the target for PKC? in LPS signaling is unknown. LPS signaling is mediated by Toll-like receptor 4, which uses four adapter proteins, MyD88, MyD88 adapter-like (Mal), Toll/IL-1R domain-containing adapter inducing IFN-? (Trif), and Trif-related adapter molecule (TRAM). Here we show that TRAM is transiently phosphorylated by PKC? on serine-16 in an LPS-dependent manner. Activation of IFN regulatory factor 3 and induction of the chemokine RANTES, which are both TRAM-dependent, were attenuated in PKC?-deficient cells. TRAMS16A is inactive when overexpressed and is attenuated in its ability to reconstitute signaling in TRAM-deficient cells. We have therefore uncovered a key process in Toll-like receptor 4 signaling, identifying TRAM as the target for PKC?.
Keyword(s): Biochemistry
Publication Date:
2006
Type: Journal article
Peer-Reviewed: Yes
Language(s): English
Institution: Trinity College Dublin
Funder(s): Health Research Board; Science Foundation Ireland
Citation(s): McGettrick, A, Brint EK, Palsson-McDermott, EM, Rowe, DC, Golenbock, DT, Gay NJ, Fitzgerald, KA and O?Neill LA `Trif-related adapter molecule is phosphorylated by protein kinase C epsilon during Toll-like receptor 4 signalling? in Proceedings of the National Academy of Sciences, 103, (24), 2006, pp 9196 - 9201
Publisher(s): National Academy of Sciences
File Format(s): application/pdf
First Indexed: 2014-05-13 05:57:38 Last Updated: 2015-04-10 05:41:09