Historical Background
The first IL-17 receptor (IL-17RA) was identified in 1995 by using the viral homolog, herpesvirus saimiri gene 13 (HVS13) (Yao et al. 1995). An Fc-HVS13 fusion protein was used to isolate cDNA from mouse T cells which encode a protein that binds all its orthologous forms. Following the discovery of mouse IL-17RA, Yao et al. isolated cDNA encoding the human IL-17RA from an activated peripheral blood leukocyte cDNA library by using mouse cDNA as a probe. The predicted 866-amino-acid type I membrane glycoprotein was 69% identical and 82% similar to the mouse sequence. It was not recognized to be related to any of the other known cytokine receptors and did not possess similarity to any other known protein nor any recognizable domains. Hence, IL-17RA and its ligand, IL-17A, represented a distinct highly conserved receptor-ligand pair. The study also showed low affinity of IL-17RA for IL-17A, lower than the concentration...
Keywords
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in via an institution.
References
Boisson B, Wang C, Pedergnana V, Wu L, Cypowyj S, Rybojad M, Belkadi A, Picard C, Abel L, Fieschi C, Puel A, Li X, Casanova JL. An ACT1 mutation selectively abolishes interleukin-17 responses in humans with chronic mucocutaneous candidiasis. Immunity. 2013;39(4):676–86.
Doyle MS, Collins ES, FitzGerald OM, Pennington SR. New insight into the functions of the interleukin-17 receptor adaptor protein Act1 in psoriatic arthritis. Arthritis Res Ther. 2012;14(5):226.
Gaffen SL. Structure and signalling in the IL-17 receptor family. Nat Rev Immunol. 2009;9:556–67.
Gaffen SL, Jain R, Garg AV, Cua DJ. The IL-23-IL-17 immune axis: from mechanisms to therapeutic testing. Nat Rev Immunol. 2014;14(9):585–600.
Gu C, Wu L, Li X. IL-17 family: cytokines, receptors and signaling. Cytokine. 2013;64(2):477–85.
Huang XD, Zhang H, He MX. Comparative and evolutionary analysis of the interleukin 17 gene family in invertebrates. PLoS One. 2015;10(7):e0132802.
Krstic J, Obradovic H, Kukolj T, Mojsilovic S, Okic-Dordevic I, Bugarski D, Santibanez JF. An overview of interleukin-17A and interleukin-17 receptor A structure. Interac Sign Protein Pept Lett. 2015;22(7):570–8.
Liu S, Ren J, Li J. IL-17RA in intestinal inflammation: structure, signaling, function, and clinical application. Inflamm Bowel Dis. 2015;21(1):154–66.
Maitra A, Shen F, Hanel W, Mossman K, Tocker J, Swart D, Gaffen SL. Distinct functional motifs within the IL-17 receptor regulate signal transduction and target gene expression. Proc Natl Acad Sci U S A. 2007;104(18):7506–11.
Mellett M, Atzei P, Bergin R, Horgan A, Floss T, Wurst W, Callanan JJ, Moynagh PN. Orphan receptor IL-17RD regulates Toll-like receptor signalling via SEFIR/TIR interactions. Nat Commun. 2015;6:6669.
Moseley TA, Haudenschild DR, Rose L, Reddi AH. Interleukin-17 family and IL-17 receptors. Cytokine Growth Factor Rev. 2003;14:155–74.
Onishi RM, Park SJ, Hanel W, Ho AW, Maitra A, Gaffen SL. SEF/IL-17R (SEFIR) is not enough: an extended SEFIR domain is required for IL-17RA-mediated signal transduction. J Biol Chem. 2010;285:32751–9.
Velichko S, Zhou X, Zhu L, Anderson JD, Wu R, Chen Y. A novel nuclear function for the interleukin-17 Signaling Adaptor Protein Act1. PLoS One. 2016;11(10):e0163323.
Wasilewska A, Winiarska M, Olszewska M, Rudnicka L. Interleukin-17 inhibitors. A new era in treatment of psoriasis and other skin diseases. Postepy Dermatol Alergol. 2016;33(4):247–52.
Wu NL, Huang DY, Tsou HN, Lin YC, Lin WW. Syk mediates IL-17-induced CCL20 expression by targeting Act1-dependent K63-linked ubiquitination of TRAF6. J Invest Dermatol. 2015;135(2):490–8.
Yao Z, Fanslow WC, Seldin MF, Rousseau AM, Painter SL, Comeau MR, Cohen JI, Spriggs MK. Herpesvirus saimiri encodes a new cytokine, IL-17, which binds to a novel cytokine receptor. Immunity. 1995;3:811–21.
Yao Z, Spriggs MK, Derry JMJ, Strockbine L, Park LS, VandenBos T, Zappone J, Painter SL, Armitage RJ. Molecular characterization of the human interleukin (IL)-17 receptor. Cytokine. 1997;9:794–800.
Zhang B, Liu C, Qian W, Han Y, Li X, Deng J. Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved α-helix for Act1 binding and IL-17 signaling. Acta Crystallogr D Biol Crystallogr. 2014;70(Pt 5):1476–83.
Acknowledgments
We apologize to those colleagues whose work, although relevant to the issues dealt within this chapter, has not been included due to space limitations. Also we appreciate OMIM (http://www.omim.org/) for the valuable compiled information. This work was supported by Grant no. 175062 from the Ministry of Education, Science and Technological Development of the Republic of Serbia.
Conflict of Interest
None to declare
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2016 Springer Science+Business Media LLC
About this entry
Cite this entry
Mojsilović, S., Trivanović, D., Krstić, J., Santibanez, J.F. (2016). Interleukin-17 Receptor A. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-6438-9_101716-1
Download citation
DOI: https://doi.org/10.1007/978-1-4614-6438-9_101716-1
Received:
Accepted:
Published:
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-6438-9
Online ISBN: 978-1-4614-6438-9
eBook Packages: Springer Reference Biomedicine and Life SciencesReference Module Biomedical and Life Sciences