Different modes of ubiquitination of the adaptor TRAF3 selectively activate the expression of type I interferons and proinflammatory cytokines View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2010-01

AUTHORS

Ping-Hui Tseng, Atsushi Matsuzawa, Weizhou Zhang, Takashi Mino, Dario A A Vignali, Michael Karin

ABSTRACT

Balanced production of type I interferons and proinflammatory cytokines after engagement of Toll-like receptors (TLRs), which signal through adaptors containing a Toll-interleukin 1 receptor (TIR) domain, such as MyD88 and TRIF, has been proposed to control the pathogenesis of autoimmune disease and tumor responses to inflammation. Here we show that TRAF3, a ubiquitin ligase that interacts with both MyD88 and TRIF, regulated the production of interferon and proinflammatory cytokines in different ways. Degradative ubiquitination of TRAF3 during MyD88-dependent TLR signaling was essential for the activation of mitogen-activated protein kinases (MAPKs) and production of inflammatory cytokines. In contrast, TRIF-dependent signaling triggered noncanonical TRAF3 self-ubiquitination that activated the interferon response. Inhibition of degradative ubiquitination of TRAF3 prevented the expression of all proinflammatory cytokines without affecting the interferon response. More... »

PAGES

70-75

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ni.1819

    DOI

    http://dx.doi.org/10.1038/ni.1819

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1011969709

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/19898473


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