Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein

Huang, Jianing; Gao, Xiong; Li, Shyun; Cao, Zhaodan

doi:10.1073/pnas.94.24.12829

Cited by 207 publications

(139 citation statements)

References 25 publications

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“…Membrane IL-1RAcP is a crucial component of the IL-1 signaling complex, stabilizing the IL-1-IL-1RI complex and mediating IL-1 signaling (7,16,17,36). The recently discovered naturally occurring alternative splice transcript of the membrane IL-1RAcP comprises the 3 extracellular Ig-like domains (4,22,23).…”

Section: Discussionmentioning

confidence: 99%

“…Another member of the IL-1 receptor family is IL-1RII (68 kd) (15), which upon binding of IL-1 also associates with IL-1RAcP. However, this does not lead to signal transduction because this receptor lacks the intracellular Toll-IL-1 receptor domain that is crucial for MyD88 binding (16)(17)(18). Therefore, the type II receptor is a decoy receptor as has been described for its transmembrane and soluble forms (19).…”

mentioning

confidence: 99%

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Soluble interleukin‐1 receptor accessory protein ameliorates collagen‐induced arthritis by a different mode of action from that of interleukin‐1 receptor antagonist

Smeets¹,

Joosten²,

Arntz³

et al. 2005

Arthritis & Rheumatism

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Objective. To discern the mode of interleukin-1 (IL-1) inhibition of soluble IL-1 receptor accessory protein (sIL-1RAcP) by comparison with IL-1 receptor antagonist (IL-1Ra) in arthritis.Methods. Adenoviral vectors encoding either sIL1RAcP or IL-1Ra were administered systemically before onset of collagen-induced arthritis in DBA/1 mice. Antibovine type II collagen IgG and IL-6 were quantified in serum. Proliferative response of splenic T cells was determined in the presence of sIL-1RAcP or IL-1Ra. The effect on IL-1 inhibition of recombinant sIL-1RAcP and IL-1Ra was further examined in vitro, using NF-B luciferase reporter cell lines. Quantitative polymerase chain reaction was used to determine the relative messenger RNA expression of the IL-1 receptors.Results. Adenoviral overexpression of both sIL1RAcP and IL-1Ra resulted in amelioration of the collagen-induced arthritis. Both IL-1 antagonists reduced the circulating levels of antigen-specific IgG2a antibodies, but only IL-1Ra was able to inhibit lymphocyte proliferation. By using purified lymphocyte populations derived from NF-B reporter mice, we showed that sIL-1RAcP inhibits IL-1-induced NF-B activity in B cells but not T cells, whereas IL-1Ra inhibited IL-1 on both cell types. A study in a panel of NF-B luciferase reporter cells showed that the sIL-1RAcP inhibits IL-1 signaling on cells expressing either low levels of membrane IL-1RAcP or high levels of IL-1RII.Conclusion. We show that the sIL-1RAcP ameliorated experimental arthritis without affecting T cell immunity, in contrast to IL-1Ra. Our results provide data in support of receptor competition by sIL-1RAcP as an explanation for the different mode of IL-1 antagonism in comparison with IL-1Ra.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Soluble interleukin‐1 receptor accessory protein ameliorates collagen‐induced arthritis by a different mode of action from that of interleukin‐1 receptor antagonist

Smeets¹,

Joosten²,

Arntz³

et al. 2005

Arthritis & Rheumatism

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“…Both groups performed biochemical and functional studies to define the molecular ordering of MyD88, IRAKs, and TRAF6 in the IL-1R1 signaling pathway. Prior to the aforementioned work, it was known that IL-1b stimulation induced a complex of IL-1R1 and IL-1RAP, leading to recruitment and phosphorylation of the IRAK kinase to the complex (21,22). The work by Wesche et al and Muzio et al showed that MyD88 was the link between IL-1R1 and IRAK to induce NF-kB activation.…”

Section: Myd88: a Critical Adaptor Protein In Innate Immunity Signalmentioning

confidence: 99%

MyD88: A Critical Adaptor Protein in Innate Immunity Signal Transduction

Warner

Núñez²

2013

The Journal of Immunology

148

122

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“…Upon binding of IL-1, the IL-1RI associates with IL-1 receptor accessory protein (IL-1RAcP), forming a functional signaling receptor complex (Fig. 1) [16,17]. Secondly, the TIR domain containing adaptor protein MyD88 is recruited to the receptor complex [18].…”

Section: Il-1r and Tlr-4 Signaling To Nf-kbmentioning

confidence: 99%

TLR-4, IL-1R and TNF-R signaling to NF-κB: variations on a common theme

Verstrepen

Bekaert

Chau

et al. 2008

Cell. Mol. Life Sci.

386

297

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Abstract. Toll-like receptors (TLRs) as well as the receptors for tumor necrosis factor (TNF-R) and interleukin-1 (IL-1R) play an important role in innate immunity by regulating the activity of distinct transcription factors such as nuclear factor-kB (NF-kB). TLR, IL-1R and TNF-R signaling to NF-kB converge on a common IkB kinase complex that phosphorylates the NF-kB inhibitory protein IkBa. However, upstream signaling components are in large part receptor-specific. Nevertheless, the principles of signaling are similar, involving the recruitment of specific adaptor proteins and the activation of kinase cascades in which protein-protein interactions are controlled by poly-ubiquitination. In this review, we will discuss our current knowledge of NF-kB signaling in response to TLR-4, TNF-R and IL-1R stimulation, with a special focus on the similarities and dissimilarities among these pathways.Keywords. Toll-like receptor 4, interleukin-1, tumor necrosis factor, NF-kB, signal transduction. NF-kB, does it still need to be introduced?Nuclear factor kB (NF-kB) is the generic name of a family of transcription factors that regulate the expression of a large number of genes involved in immune and inflammatory responses, as well as in cell survival, cell proliferation and cell differentiation. NFkB transcription factors are activated in response to various stimuli, including cytokines, infectious agents, injury and other stressful conditions requiring rapid reprogramming of gene expression. Inappropriate activation of the NF-kB signaling pathway is implicated in the pathogenesis of chronic inflammation and autoimmunity, certain hereditary disorders and various cancers. In mammals, the NF-kB family consists of five proteins sharing a highly conserved Rel homology domain: c-Rel, RelB, p65 (= RelA), p105 (= NF-kB1) and p100 (=NF-kB2). The first three contain Cterminal transactivation domains, while the others share a long C-terminal domain with multiple copies of ankyrin repeats, which inhibit their activation.

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Recruitment of IRAK to the interleukin 1 receptor complex requires interleukin 1 receptor accessory protein

Abstract: The proinf lammatory cytokine interleukin 1 (IL- 1

Cited by 207 publications

References 25 publications

Soluble interleukin‐1 receptor accessory protein ameliorates collagen‐induced arthritis by a different mode of action from that of interleukin‐1 receptor antagonist

Soluble interleukin‐1 receptor accessory protein ameliorates collagen‐induced arthritis by a different mode of action from that of interleukin‐1 receptor antagonist

MyD88: A Critical Adaptor Protein in Innate Immunity Signal Transduction

TLR-4, IL-1R and TNF-R signaling to NF-κB: variations on a common theme

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