Arrestin beta 2

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Arrestin, beta 2
Identifiers
Symbols ARRB2 ; ARB2; ARR2; DKFZp686L0365
External IDs Template:OMIM5 Template:MGI HomoloGene3183
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Arrestin, beta 2, also known as ARRB2, is a human gene.

Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.[1]

References

  1. "Entrez Gene: ARRB2 arrestin, beta 2".

Further reading

  • Lefkowitz RJ (1998). "G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization". J. Biol. Chem. 273 (30): 18677–80. PMID 9668034.
  • Attramadal H, Arriza JL, Aoki C; et al. (1992). "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family". J. Biol. Chem. 267 (25): 17882–90. PMID 1517224.
  • Rapoport B, Kaufman KD, Chazenbalk GD (1992). "Cloning of a member of the arrestin family from a human thyroid cDNA library". Mol. Cell. Endocrinol. 84 (3): R39–43. PMID 1587386.
  • Calabrese G, Sallese M, Stornaiuolo A; et al. (1995). "Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes". Genomics. 23 (1): 286–8. doi:10.1006/geno.1994.1497. PMID 7695743.
  • Parruti G, Peracchia F, Sallese M; et al. (1993). "Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing". J. Biol. Chem. 268 (13): 9753–61. PMID 8486659.
  • Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J (1997). "Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor". FEBS Lett. 402 (2–3): 203–8. PMID 9037196.
  • Barak LS, Ferguson SS, Zhang J, Caron MG (1997). "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation". J. Biol. Chem. 272 (44): 27497–500. PMID 9346876.
  • Laporte SA, Oakley RH, Zhang J; et al. (1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. PMID 10097102.
  • Cheng ZJ, Zhao J, Sun Y; et al. (2000). "beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4". J. Biol. Chem. 275 (4): 2479–85. PMID 10644702.
  • Lin F, Wang H, Malbon CC (2000). "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". J. Biol. Chem. 275 (25): 19025–34. PMID 10858453.
  • McDonald PH, Chow CW, Miller WE; et al. (2000). "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science. 290 (5496): 1574–7. PMID 11090355.
  • Luttrell LM, Roudabush FL, Choy EW; et al. (2001). "Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds". Proc. Natl. Acad. Sci. U.S.A. 98 (5): 2449–54. doi:10.1073/pnas.041604898. PMID 11226259.
  • Cen B, Yu Q, Guo J; et al. (2001). "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". J. Neurochem. 76 (6): 1887–94. PMID 11259507.
  • Oakley RH, Laporte SA, Holt JA; et al. (2001). "Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*". J. Biol. Chem. 276 (22): 19452–60. doi:10.1074/jbc.M101450200. PMID 11279203.
  • Miller WE, McDonald PH, Cai SF; et al. (2001). "Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3". J. Biol. Chem. 276 (30): 27770–7. doi:10.1074/jbc.M102264200. PMID 11356842.
  • Claing A, Chen W, Miller WE; et al. (2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45): 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.
  • Hilairet S, Bélanger C, Bertrand J; et al. (2001). "Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin". J. Biol. Chem. 276 (45): 42182–90. doi:10.1074/jbc.M107323200. PMID 11535606.
  • Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ (2001). "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin". Science. 294 (5545): 1307–13. doi:10.1126/science.1063866. PMID 11588219.
  • Chen Z, Dupré DJ, Le Gouill C; et al. (2002). "Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif". J. Biol. Chem. 277 (9): 7356–62. doi:10.1074/jbc.M110058200. PMID 11729201.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.