Interleukin 8 receptor, beta

Interleukin 8 receptor, beta

Chemokine (C-X-C motif) receptor 2
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; CD182; CDw128b; CMKAR2; IL8R2; IL8RA; IL8RB
External IDs IUPHAR: ChEMBL: GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Interleukin 8 receptor, beta is a chemokine receptor. IL8RB is also known as CXCR2, and CXCR2 is now the IUPHAR Committee on Receptor Nomenclature and Drug classification-recommended name.[1]


  • Function 1
  • Senescence 2
  • See also 3
  • References 4
  • External links 5
  • Further reading 6
  • External links 7


The protein encoded by this gene is a member of the G-protein-coupled receptor family. This protein is a receptor for interleukin 8 (IL8). It binds to IL8 with high affinity, and transduces the signal through a G-protein-activated second messenger system (Gi/o-coupled[2]). This receptor also binds to chemokine (C-X-C motif) ligand 1 (CXCL1/MGSA), a protein with melanoma growth stimulating activity, and has been shown to be a major component required for serum-dependent melanoma cell growth. In addition, it binds ligands CXCL2, CXCL3, and CXCL5.

This receptor mediates neutrophil migration to sites of inflammation. The angiogenic effects of IL8 in intestinal microvascular endothelial cells are found to be mediated by this receptor. Knockout studies in mice suggested that this receptor controls the positioning of oligodendrocyte precursors in developing spinal cord by arresting their migration. This gene, IL8RA, a gene encoding another high affinity IL8 receptor, and IL8RBP, a pseudogene of IL8RB, form a gene cluster in a region mapped to chromosome 2q33-q36.[3]

Mutations in CXCR2 cause hematological traits .[4]


Knock-down studies involving the chemokine receptor CXCR2 alleviates both replicative and oncogene-induced senescence (OIS) and diminishes the DNA-damage response. Also, ectopic expression of CXCR2 results in premature senescence via a p53-dependent mechanism.[5]

See also


  1. ^ Morris SW, Nelson N, Valentine MB, Shapiro DN, Look AT, Kozlosky CJ, Beckmann MP, Cerretti DP (November 1992). "Assignment of the genes encoding human interleukin-8 receptor types 1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35". Genomics 14 (3): 685–91.  
  2. ^ "Entry in: gpDB, database of GPCRs, G-proteins, Effectors and their interactions". Retrieved 3 October 2012. 
  3. ^ "Entrez Gene: IL8RB interleukin 8 receptor, beta". 
  4. ^ Auer, P. L.; Teumer, A; Schick, U; O'Shaughnessy, A; Lo, K. S.; Chami, N; Carlson, C; De Denus, S; Dubé, M. P.; Haessler, J; Jackson, R. D.; Kooperberg, C; Perreault, L. P.; Nauck, M; Peters, U; Rioux, J. D.; Schmidt, F; Turcot, V; Völker, U; Völzke, H; Greinacher, A; Hsu, L; Tardif, J. C.; Diaz, G. A.; Reiner, A. P.; Lettre, G (2014). "Rare and low-frequency coding variants in CXCR2 and other genes are associated with hematological traits". Nature Genetics 46 (6): 629–34.  
  5. ^ Acosta JC, O'Loghlen A, Banito A, Guijarro MV, Augert A, Raguz S, Fumagalli M, Da Costa M, Brown C, Popov N, Takatsu Y, Melamed J, d'Adda di Fagagna F, Bernard D, Hernando E, Gil J. (June 2008). "Chemokine Signaling via the CXCR2 Receptor Reinforces Senescence.". Cell. 133 (6): 1006–18.  

External links

  • "Chemokine Receptors: CXCR2". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. 

Further reading

  • Brandt E, Ludwig A, Petersen F, Flad HD (2001). "Platelet-derived CXC chemokines: old players in new games.". Immunol. Rev. 177: 204–16.  
  • Robertson MJ (2002). "Role of chemokines in the biology of natural killer cells.". J. Leukoc. Biol. 71 (2): 173–83.  
  • Ahuja SK, Ozçelik T, Milatovitch A, et al. (1993). "Molecular evolution of the human interleukin-8 receptor gene cluster.". Nat. Genet. 2 (1): 31–6.  
  • Lee J, Horuk R, Rice GC, et al. (1992). "Characterization of two high affinity human interleukin-8 receptors.". J. Biol. Chem. 267 (23): 16283–7.  
  • Morris SW, Nelson N, Valentine MB, et al. (1992). "Assignment of the genes encoding human interleukin-8 receptor types 1 and 2 and an interleukin-8 receptor pseudogene to chromosome 2q35.". Genomics 14 (3): 685–91.  
  • Holmes WE, Lee J, Kuang WJ, et al. (1991). "Structure and functional expression of a human interleukin-8 receptor.". Science 253 (5025): 1278–80.  
  • Murphy PM, Tiffany HL (1991). "Cloning of complementary DNA encoding a functional human interleukin-8 receptor.". Science 253 (5025): 1280–3.  
  • Sprenger H, Lloyd AR, Lautens LL, et al. (1994). "Structure, genomic organization, and expression of the human interleukin-8 receptor B gene.". J. Biol. Chem. 269 (15): 11065–72.  
  • Morohashi H, Miyawaki T, Nomura H, et al. (1995). "Expression of both types of human interleukin-8 receptors on mature neutrophils, monocytes, and natural killer cells.". J. Leukoc. Biol. 57 (1): 180–7.  
  • Ahuja SK, Shetty A, Tiffany HL, Murphy PM (1994). "Comparison of the genomic organization and promoter function for human interleukin-8 receptors A and B.". J. Biol. Chem. 269 (42): 26381–9.  
  • Cacalano G, Lee J, Kikly K, et al. (1994). "Neutrophil and B cell expansion in mice that lack the murine IL-8 receptor homolog.". Science 265 (5172): 682–4.  
  • Harada A, Kuno K, Nomura H, et al. (1994). "Cloning of a cDNA encoding a mouse homolog of the interleukin-8 receptor.". Gene 142 (2): 297–300.  
  • Schnitzel W, Monschein U, Besemer J (1994). "Monomer-dimer equilibria of interleukin-8 and neutrophil-activating peptide 2. Evidence for IL-8 binding as a dimer and oligomer to IL-8 receptor B.". J. Leukoc. Biol. 55 (6): 763–70.  
  • Mueller SG, Schraw WP, Richmond A (1994). "Melanoma growth stimulatory activity enhances the phosphorylation of the class II interleukin-8 receptor in non-hematopoietic cells.". J. Biol. Chem. 269 (3): 1973–80.  
  • Wu D, LaRosa GJ, Simon MI (1993). "G protein-coupled signal transduction pathways for interleukin-8.". Science 261 (5117): 101–3.  
  • Cerretti DP, Kozlosky CJ, Vanden Bos T, et al. (1993). "Molecular characterization of receptors for human interleukin-8, GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-2.". Mol. Immunol. 30 (4): 359–67.  
  • Ahuja SK, Lee JC, Murphy PM (1996). "CXC chemokines bind to unique sets of selectivity determinants that can function independently and are broadly distributed on multiple domains of human interleukin-8 receptor B. Determinants of high affinity binding and receptor activation are distinct.". J. Biol. Chem. 271 (1): 225–32.  
  • Hammond ME, Shyamala V, Siani MA, et al. (1996). "Receptor recognition and specificity of interleukin-8 is determined by residues that cluster near a surface-accessible hydrophobic pocket.". J. Biol. Chem. 271 (14): 8228–35.  
  • Damaj BB, McColl SR, Mahana W, et al. (1996). "Physical association of Gi2alpha with interleukin-8 receptors.". J. Biol. Chem. 271 (22): 12783–9.  
  • Ahuja SK, Murphy PM (1996). "The CXC chemokines growth-regulated oncogene (GRO) alpha, GRObeta, GROgamma, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil-activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor.". J. Biol. Chem. 271 (34): 20545–50.  

External links