Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors

  title={Triad3A, an E3 ubiquitin-protein ligase regulating Toll-like receptors},
  author={Tsung-Hsien Chuang and Richard J Ulevitch},
  journal={Nature Immunology},
Activation of Toll-like receptors (TLRs) results in a proinflammatory response needed to combat infection. Thus, limiting TLR signaling is essential for preventing a protective response from causing injury to the host. Here we describe how a RING finger protein, Triad3A, acts as an E3 ubiquitin-protein ligase and enhances ubiquitination and proteolytic degradation of some TLRs. Triad3A overexpression promoted substantial degradation of TLR4 and TLR9 with a concomitant decrease in signaling, but… 

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Upregulation of costimulatory molecules induced by lipopolysaccharide and double-stranded RNA occurs by Trif-dependent and Trif-independent pathways

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Lipopolysaccharide Is in Close Proximity to Each of the Proteins in Its Membrane Receptor Complex

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A Novel Pathway Regulating Lipopolysaccharide-Induced Shock by ST2/T1 Via Inhibition of Toll-Like Receptor 4 Expression1

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Mechanisms underlying ubiquitination.

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Recent findings reveal that all known E3s utilize one of just two catalytic domains--a HECT domain or a RING finger--and crystal structures have provided the first detailed views of an active site of each type.

Toll-like receptors as potential therapeutic targets for multiple diseases

The current and future use of TLR agonists or antagonists in chronic inflammatory diseases are discussed and potential problems that are associated with such approaches are highlighted.