Arrestin beta 2

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Arrestin beta 2

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Arrestin, beta 2

Identifiers

Symbols

ARRB2; ARB2; ARR2; BARR2; DKFZp686L0365

External IDs

OMIM: 107941 MGI: 99474 HomoloGene: 3183 GeneCards: ARRB2 Gene

Gene Ontology
Molecular function	• G-protein-coupled receptor binding • receptor binding • protein binding • ubiquitin protein ligase binding • angiotensin receptor binding • protein kinase B binding
Cellular component	• intracellular • nucleus • cytoplasm • cytosol • plasma membrane • coated pit • cytoplasmic membrane-bounded vesicle • cytoplasmic vesicle
Biological process	• regulation of protein phosphorylation • G-protein coupled receptor internalization • G-protein coupled receptor internalization • desensitization of G-protein coupled receptor protein signaling pathway by arrestin • transcription from RNA polymerase II promoter • transforming growth factor beta receptor signaling pathway • blood coagulation • adult walking behavior • regulation of G-protein coupled receptor protein signaling pathway • protein transport • protein ubiquitination • platelet activation • negative regulation of protein ubiquitination • receptor internalization • negative regulation of NF-kappaB transcription factor activity • positive regulation of synaptic transmission, dopaminergic • negative regulation of interleukin-1 beta production • negative regulation of interleukin-12 production • negative regulation of interleukin-6 production • negative regulation of tumor necrosis factor production • negative regulation of toll-like receptor signaling pathway • proteasomal ubiquitin-dependent protein catabolic process • negative regulation of natural killer cell mediated cytotoxicity • positive regulation of protein kinase B signaling cascade • cell chemotaxis • positive regulation of ERK1 and ERK2 cascade • positive regulation of ERK1 and ERK2 cascade
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
4.61 – 4.62 Mb

Chr 11:
70.25 – 70.25 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-HT_2A receptor signaling.^[10]^[11]

Interactions

Arrestin beta 2 has been shown to interact with

References

^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2751575.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2672012.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2253657.
^ 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.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2268080.
^ 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.
^ 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.
^ 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.
^ "Entrez Gene: ARRB2 arrestin, beta 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=409.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2242710.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2242676.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22359.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2494938.
^ 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.

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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22359.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=30158.
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.

This article on a gene on chromosome 17 is a stub. You can help Wikipedia by expanding it.

v · d · eProtein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin	SAG, ARRB1, ARRB2, ARR3

Membrane-spanning 4A	MS4A1 · MS4A2 · MS4A3 · MS4A4A · MS4A4E · MS4A5 · MS4A6A · MS4A6E · MS4A7 · MS4A8B · MS4A9 · MS4A10 · MS4A12 · MS4A13 · MS4A14 · MS4A15 · MS4A18

Myelin	Myelin basic protein (PMP2) · Myelin proteolipid protein (PLP1) · Myelin oligodendrocyte glycoprotein · Myelin-associated glycoprotein · Myelin protein zero

Pulmonary surfactant	Pulmonary surfactant-associated protein B · Pulmonary surfactant-associated protein C

Tetraspanin	TSPAN1 · TSPAN2 · TSPAN3 · TSPAN4 · TSPAN5 · TSPAN6 · TSPAN7 · TSPAN8 · TSPAN9 · TSPAN10 · TSPAN11 · TSPAN12 · TSPAN13 · TSPAN14 · TSPAN15 · TSPAN16 · TSPAN17 · TSPAN18 · TSPAN19 · TSPAN20 · TSPAN21 · TSPAN22 · TSPAN23 · TSPAN24 · TSPAN25 · TSPAN26 · TSPAN27 · TSPAN28 · TSPAN29 · TSPAN30 · TSPAN31 · TSPAN32 · TSPAN33 · TSPAN34

Other/ungrouped	Calnexin · LDL-receptor-related protein associated protein · Neurofibromin 2 · Presenilin (PSEN1, PSEN2) · HFE · Phospholipid transfer proteins · Dysferlin · STRC · OTOF

see also other cell membrane protein disorders B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr

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