Structural and functional attributes of the interleukin-36 receptor

Journal of Biological Chemistry

Volumn 291, Issue 32, 2016, Pages 16597-16609

  Yi, Guanghui ^a   Ybe, Joel A ^a   Saha, Siddhartha S ^a   Caviness, Gary ^b   Raymond, Ernest ^b   Ganesan, Rajkumar ^b   Mbow, M Lamine ^b   Kao, C Cheng ^a  

^a INDIANA UNIVERSITY   (United States)

^b BOEHRINGER INGELHEIM PHARMACEUTICALS INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSAYS; BACTERIOPHAGES; COVALENT BONDS; SULFUR COMPOUNDS;

DISULFIDE BOND FORMATION; DOMINANT NEGATIVE; FUNCTIONAL ASSAYS; FUNCTIONAL ATTRIBUTE; HUMAN POPULATION; MUTATIONAL ANALYSIS; PROTEIN EXPRESSIONS; SINGLE NUCLEOTIDE POLYMORPHISMS;

SIGNAL TRANSDUCTION;

INTERLEUKIN 1 RECEPTOR ACCESSORY PROTEIN; INTERLEUKIN 1 RECEPTOR TYPE II; INTERLEUKIN 36 RECEPTOR; INTERLEUKIN RECEPTOR; UNCLASSIFIED DRUG; IL18R1 PROTEIN, HUMAN; IL1RAP PROTEIN, HUMAN; INTERLEUKIN 18 RECEPTOR ALPHA;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL ASSAY; CELL BASED REPORTER ASSAY; CONTROLLED STUDY; DISULFIDE BOND; DOWN REGULATION; MOLECULAR MODEL; MOLECULAR RECOGNITION; MUTATIONAL ANALYSIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTEIN SUBUNIT; RESIDUE ANALYSIS; SIGNAL TRANSDUCTION; SINGLE NUCLEOTIDE POLYMORPHISM; STABLE EXPRESSION; STRUCTURE ANALYSIS; CHEMISTRY; GENETIC POLYMORPHISM; GENETICS; HEK293 CELL LINE; HUMAN; METABOLISM; STRUCTURE ACTIVITY RELATION;

HEK293 CELLS; HUMANS; INTERLEUKIN-1 RECEPTOR ACCESSORY PROTEIN; INTERLEUKIN-18 RECEPTOR ALPHA SUBUNIT; POLYMORPHISM, GENETIC; PROTEIN DOMAINS; SIGNAL TRANSDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84982836652     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M116.723064     Document Type: Article

References (30)

1. Towne, J. E., and Sims, J. E. (2012) IL-36 in psoriasis. Curr. Opin. Pharmacol. 12, 486-490
2. Gresnigt, M. S., and van de Veerdonk, F. L. (2013) Biology of IL-36 cytokines and their role in disease. Semin. Immunol. 25, 458-465
3. Blumberg, H., Dinh, H., Trueblood, E. S., Pretorius, J., Kugler, D., Weng, N., Kanaly, S. T., Towne, J. E., Willis, C. R., Kuechle, M. K., Sims, J. E., and Peschon, J. J. (2007) Opposing activities of two novel members of the IL-1 ligand family regulate skin inflammation. J. Exp. Med. 204, 2603-2614
4. Gabay, C., and Towne, J. E. (2015) Regulation and function of interleukin-36 cytokines in homeostasis and pathological conditions. J. Leukoc. Biol. 97, 645-652
5. Medina-Contreras, O., Harusato, A., Nishio, H., Flannigan, K. L., Ngo, V., Leoni, G., Neumann, P. A., Geem, D., Lili, L. N., Ramadas, R. A., Chassaing, B., Gewirtz, A. T., Kohlmeier, J. E., Parkos, C. A., Towne, J. E., Nusrat, A., and Denning, T. L. (2016) Cutting Edge: IL-36 Receptor Promotes Resolution of Intestinal Damage. J. Immunol. 196, 34-38
6. Foster, A. M., Baliwag, J., Chen, C. S., Guzman, A. M., Stoll, S. W., Gudjonsson, J. E., Ward, N. L., and Johnston, A. (2014) IL-36 promotes myeloid cell infiltration, activation, and inflammatory activity in skin. J. Immunol. 192, 6053-6061
7. Garlanda, C., Dinarello, C. A., and Mantovani, A. (2013) The interleukin-1 family: back to the future. Immunity 39, 1003-1018
8. Towne, J. E., Garka, K. E., Renshaw, B. R., Virca, G. D., and Sims, J. E. (2004) Interleukin (IL)-1F6, IL-1F8, and IL-1F9 signal through IL-1Rrp2 and IL-1RAcP to activate the pathway leading to NF-κB and MAPKs. J. Biol. Chem. 279, 13677-13688
9. Towne, J. E., Renshaw, B. R., Douangpanya, J., Lipsky, B. P., Shen, M., Gabel, C. A., and Sims, J. E. (2011) Interleukin-36 (IL-36) ligands require processing for full agonist (IL-36α, IL-36β, and IL-36γ) or antagonist (IL-36Ra) activity. J. Biol. Chem. 286, 42594-42602
10. Debets, R., Timans, J. C., Homey, B., Zurawski, S., Sana, T. R., Lo, S., Wagner, J., Edwards, G., Clifford, T., Menon, S., Bazan, J. F., and Kastelein, R. A. (2001) Two novel IL-1 family members, IL-1 delta and IL-1 epsilon, function as an antagonist and agonist of NF-κB activation through the orphan IL-1 receptor-related protein 2. J. Immunol. 167, 1440-1446
11. van de Veerdonk, F. L., Stoeckman, A. K., Wu, G., Boeckermann, A. N., Azam, T., Netea, M. G., Joosten, L. A., van der Meer, J. W., Hao, R., Kalabokis, V., and Dinarello, C. A. (2012) IL-38 binds to the IL-36 receptor and has biological effects on immune cells similar to IL-36 receptor antagonist. Proc. Natl. Acad. Sci. U.S.A. 109, 3001-3005
12. Thomas, C., Bazan, J. F., and Garcia, K. C. (2012) Structure of the activating IL-1 receptor signaling complex. Nat. Struct. Mol. Biol. 19, 455-457
13. Wang, D., Zhang, S., Li, L., Liu, X., Mei, K., and Wang, X. (2010) Structural insights into the assembly and activation of IL-1β with its receptors. Nat. Immunol. 11, 905-911
14. Tsutsumi, N., Kimura, T., Arita, K., Ariyoshi, M., Ohnishi, H., Yamamoto, T., Zuo, X., Maenaka, K., Park, E. Y., Kondo, N., Shirakawa, M., Tochio, H., and Kato, Z. (2014) The structural basis for receptor recognition of human interleukin-18. Nat. Commun. 5, 5340
15. Liu, X., Hammel, M., He, Y., Tainer, J. A., Jeng, U. S., Zhang, L., Wang, S., and Wang, X. (2013) Structural insights into the interaction of IL-33 with its receptors. Proc. Natl. Acad. Sci. U.S.A. 110, 14918-14923
16. Günther, S., and Sundberg, E. J. (2014) Molecular determinants of agonist and antagonist signaling through the IL-36 receptor. J. Immunol. 193, 921-930
17. Deribe, Y. L., Pawson, T., and Dikic, I. (2010) Post-translational modifications in signal integration. Nat. Struct. Mol. Biol. 17, 666-672
18. Saha, S. S., Singh, D., Raymond, E. L., Ganesan, R., Caviness, G., Grimaldi, C., Woska, J. R., Jr., Mennerich, D., Brown, S. E., Mbow, M. L., and Kao, C. C. (2015) Signal transduction and intracellular trafficking by the interleukin 36 receptor. J. Biol. Chem. 290, 23997-24006
19. Hornung, V., Rothenfusser, S., Britsch, S., Krug, A., Jahrsdörfer, B., Giese, T., Endres, S., and Hartmann, G. (2002) Quantitative expression of toll-like receptor 1-10 mRNA in cellular subsets of human peripheral blood mononuclear cells and sensitivity to CpG oligodeoxynucleotides. J. Immunol. 168, 4531-4537
20. Moremen, K. W., Tiemeyer, M., and Nairn, A. V. (2012) Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13, 448-462
21. Moffatt, M. F., Gut, I. G., Demenais, F., Strachan, D. P., Bouzigon, E., Heath, S., von Mutius, E., Farrall, M., Lathrop, M., Cookson, W. O., and Gabriel Consortium (2010) A large-scale, consortium-based genomewide association study of asthma. New Eng. J. Med. 363, 1211-1221
22. Latiano, A., Palmieri, O., Pastorelli, L., Vecchi, M., Pizarro, T. T., Bossa, F., Merla, G., Augello, B., Latiano, T., Corritore, G., Settesoldi, A., Valvano, M. R., D'Incà, R., Stronati, L., Annese, V., and Andriulli, A. (2013) Associations between genetic polymorphisms in IL-33, IL1R1 and risk for inflammatory bowel disease. PloS one 8, e62144
23. Wesche, H., Henzel, W. J., Shillinglaw, W., Li, S., and Cao, Z. (1997) MyD88: an adapter that recruits IRAK to the IL-1 receptor complex. Immunity 7, 837-847
24. Dunne, A., and O'Neill, L. A. (2003) The interleukin-1 receptor/Toll-like receptor superfamily: signal transduction during inflammation and host defense. Science's STKE: Sig. Trans. re3
25. Jiang, Z., Georgel, P., Li, C., Choe, J., Crozat, K., Rutschmann, S., Du, X., Bigby, T., Mudd, S., Sovath, S., Wilson, I. A., Olson, A., and Beutler, B. (2006) Details of Toll-like receptor:adapter interaction revealed by germline mutagenesis. Proc. Natl. Acad. Sci. U.S.A. 103, 10961-10966
26. Livak, K. J., and Schmittgen, T. D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-ΔΔC(T)) method. Methods 25, 402-408
27. Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N., and Sternberg, M. J. (2015) The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10, 845-858
28. Kuznetsov, I. B., and McDuffie, M. (2008) FlexPred: a web-server for predicting residue positions involved in conformational switches in proteins. Bioinformatics 3, 134-136
29. Ray, A., Lindahl, E., and Wallner, B. (2012) Improved model quality assessment using ProQ2. BMC Bioinformatics 13, 224
30. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., 3rd, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383