Trif-related adapter molecule is phosphorylated by PKCε during Toll-like receptor 4 signaling

  • Anne F. McGettrick
  • , Elizabeth K. Brint
  • , Eva M. Palsson-McDermott
  • , Daniel C. Rowe
  • , Douglas T. Golenbock
  • , Nicholas J. Gay
  • , Katherine A. Fitzgerald
  • , Luke A.J. O'Neill

Research output: Contribution to journalArticlepeer-review

Abstract

PKCε has been shown to play a key role in the effect of the Gram-negative bacterial product LPS; however, the target for PKCε 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-β (Trif), and Trif-related adapter molecule (TRAM). Here we show that TRAM is transiently phosphorylated by PKCε 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 PKCε-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 PKCε.

Original languageEnglish
Pages (from-to)9196-9201
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume103
Issue number24
DOIs
Publication statusPublished - 13 Jun 2006
Externally publishedYes

Keywords

  • Innate immunity
  • LPS
  • Myristoylation

Fingerprint

Dive into the research topics of 'Trif-related adapter molecule is phosphorylated by PKCε during Toll-like receptor 4 signaling'. Together they form a unique fingerprint.

Cite this