Arrestin beta 2

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Arrestin, beta 2
Identifiers
Symbols ARRB2 ; ARB2; ARR2; BARR2
External IDs OMIM107941 MGI99474 HomoloGene3183 GeneCards: ARRB2 Gene
RNA expression pattern
PBB GE ARRB2 203388 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 409 216869
Ensembl ENSG00000141480 ENSMUSG00000060216
UniProt P32121 Q91YI4
RefSeq (mRNA) NM_001257328 NM_001271358
RefSeq (protein) NP_001244257 NP_001258287
Location (UCSC) Chr 17:
4.61 – 4.62 Mb
Chr 11:
70.43 – 70.44 Mb
PubMed search [1] [2]

Beta-arrestin-2, also known as arrestin beta-2, is an intracellular protein that in humans is encoded by the ARRB2 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,[1][2][3] as well as having signalling roles in their own right.[4][5][6][7][8] 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.[9]

The protein may interact with the agonist DOI in 5-HT2A receptor signaling.[10][11]

Interactions[edit]

Arrestin beta 2 has been shown to interact with

References[edit]

  1. ^ Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK (July 2008). "Sensitivity to Δ9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2-/- mice". Behavioural Pharmacology 19 (4): 298–307. doi:10.1097/FBP.0b013e328308f1e6. PMC 2751575. PMID 18622177. 
  2. ^ Li Y, Liu X, Liu C, Kang J, Yang J, Pei G, Wu C (March 2009). "Improvement of Morphine-Mediated Analgesia by Inhibition of β-Arrestin 2 Expression in Mice Periaqueductal Gray Matter". International Journal of Molecular Sciences 10 (3): 954–63. doi:10.3390/ijms10030954. PMC 2672012. PMID 19399231. 
  3. ^ Zheng H, Loh HH, Law PY (January 2008). "β-Arrestin-Dependent μ-Opioid Receptor-Activated Extracellular Signal-Regulated Kinases (ERKs) Translocate to Nucleus in Contrast to G Protein-Dependent ERK Activation". Molecular Pharmacology 73 (1): 178–90. doi:10.1124/mol.107.039842. PMC 2253657. PMID 17947509. 
  4. ^ Ma L, Pei G (January 2007). "Beta-arrestin signaling and regulation of transcription". Journal of Cell Science 120 (Pt 2): 213–8. doi:10.1242/jcs.03338. PMID 17215450. 
  5. ^ Defea K (March 2008). "β-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction". British Journal of Pharmacology. 153 Suppl 1 (S1): S298–309. doi:10.1038/sj.bjp.0707508. PMC 2268080. PMID 18037927. 
  6. ^ Barki-Harrington L, Rockman HA (February 2008). "Beta-arrestins: multifunctional cellular mediators". Physiology (Bethesda, Md.) 23: 17–22. doi:10.1152/physiol.00042.2007. PMID 18268361. 
  7. ^ Patel PA, Tilley DG, Rockman HA (March 2009). "Physiologic and cardiac roles of beta-arrestins". Journal of Molecular and Cellular Cardiology 46 (3): 300–8. doi:10.1016/j.yjmcc.2008.11.015. PMID 19103204. 
  8. ^ Golan M, Schreiber G, Avissar S (2009). "Antidepressants, beta-arrestins and GRKs: from regulation of signal desensitization to intracellular multifunctional adaptor functions". Current Pharmaceutical Design 15 (14): 1699–708. doi:10.2174/138161209788168038. PMID 19442183. 
  9. ^ "Entrez Gene: ARRB2 arrestin, beta 2". 
  10. ^ Schmid CL, Raehal KM, Bohn LM (January 2008). "Agonist-directed signaling of the serotonin 2A receptor depends on β-arrestin-2 interactions in vivo". Proc. Natl. Acad. Sci. U.S.A. 105 (3): 1079–84. doi:10.1073/pnas.0708862105. PMC 2242710. PMID 18195357. 
  11. ^ Abbas A, Roth BL (January 2008). "Arresting serotonin". Proc. Natl. Acad. Sci. U.S.A. 105 (3): 831–2. doi:10.1073/pnas.0711335105. PMC 2242676. PMID 18195368. 
  12. ^ Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS (March 1999). "The β2-adrenergic receptor/βarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102. 
  13. ^ Kim YM, Benovic JL (August 2002). "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking". J. Biol. Chem. 277 (34): 30760–8. doi:10.1074/jbc.M204528200. PMID 12070169. 
  14. ^ Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (November 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. 
  15. ^ Wang P, Gao H, Ni Y, Wang B, Wu Y, Ji L, Qin L, Ma L, Pei G (February 2003). "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2". J. Biol. Chem. 278 (8): 6363–70. doi:10.1074/jbc.M210350200. PMID 12488444. 
  16. ^ Wang P, Wu Y, Ge X, Ma L, Pei G (March 2003). "Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus". J. Biol. Chem. 278 (13): 11648–53. doi:10.1074/jbc.M208109200. PMID 12538596. 
  17. ^ Shenoy SK, Xiao K, Venkataramanan V, Snyder PM, Freedman NJ, Weissman AM (August 2008). "Nedd4 Mediates Agonist-dependent Ubiquitination, Lysosomal Targeting, and Degradation of the β2-Adrenergic Receptor". J. Biol. Chem. 283 (32): 22166–76. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533. 
  18. ^ Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, Feldman RD, Verdi JM, Rylett RJ, Ferguson SS (August 2002). "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nat. Cell Biol. 4 (8): 547–55. doi:10.1038/ncb821. PMID 12105416. 

Further reading[edit]

  • 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. doi:10.1074/jbc.273.30.18677. 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. doi:10.1016/0303-7207(92)90038-8. 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. doi:10.1016/S0014-5793(96)01531-1. 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. doi:10.1074/jbc.272.44.27497. PMID 9346876. 
  • Laporte SA, Oakley RH, Zhang J et al. (1999). "The β2-adrenergic receptor/βarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. doi:10.1073/pnas.96.7.3712. PMC 22359. 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. doi:10.1074/jbc.275.4.2479. 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. doi:10.1074/jbc.275.25.19025. 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. doi:10.1126/science.290.5496.1574. PMID 11090355. 
  • Luttrell LM, Roudabush FL, Choy EW et al. (2001). "Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds". Proc. Natl. Acad. Sci. U.S.A. 98 (5): 2449–54. doi:10.1073/pnas.041604898. PMC 30158. 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. doi:10.1046/j.1471-4159.2001.00204.x. 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.