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The interleukin-1 receptor family

Boraschi, Diana, Tagliabue, Aldo·2013·Seminars in Immunology
DOI 10.1016/j.smim.2013.10.023
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Abstract

The activity of each member of the IL-1 family of ligands is mediated by its own receptor. Each ligand binds specifically to the extracellular "ligand binding chain" containing three Ig-like regions. With the exception of the IL-1 and IL-36 receptor antagonists, a second chain, termed the "accessory chain", is recruited, forms a heterotrimetic complex with the ligand binding chain and the ligand, and signal transduction is initiated. Each ligand binding or accessory chain shares a common cytosolic segment termed the Toll-IL-1-receptor (TIR) domain. Another family of 13 receptors, termed Toll-like receptors (TLR), have extracellular leucine-rich repeat domains, which bind a broad spectrum of microbial products. All TLR share a nearly identical TIR domain with all members of the IL-1 receptor family. Hence signal transduction and the biological consequences of TLR ligands and IL-1 family ligands are often the same and both receptor families contribute to innate inflammation and host defense. The IL-1 family of receptors is comprised of ten distinct but related gene products. The receptors are indicated by the term IL-1 receptor (IL-1R) followed by a numeral, assigned chronologically by discovery, for example, IL-1R1, IL-1R2, IL-1R3, etc. The ligand binding chain for IL-1α and IL-1β is IL-1R1 and the accessory chain is IL-1R3. IL-1α, IL-1β, IL-33 and IL-36 use IL-1R3 as their accessory chain. IL-1R2 is a non-signalling "decoy" receptor that sequesters the IL-1β and IL-1R3. IL-1R…

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Metadata

Authors
Boraschi, D., & Tagliabue, A.
Venue
Seminars in Immunology
Publisher
Elsevier BV
Published
2013-12
Volume
25
Issue
6
Pages
394-407
ISSN
1044-5323
DOI
10.1016/j.smim.2013.10.023
Cited by
227
References
6
Language
en

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