Arrestin beta 2

ARRB2
Identifiers
Aliases	ARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
External IDs	OMIM: 107941; MGI: 99474; HomoloGene: 3183; GeneCards: ARRB2; OMA:ARRB2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17p13.2 Start 4,710,596 bp End 4,721,499 bp
Gene location (Mouse) Chr. Chromosome 11 (mouse) Band 11 B3|11 42.99 cM Start 70,323,461 bp End 70,331,654 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte monocyte right lung spleen right hemisphere of cerebellum upper lobe of left lung blood bone marrow cells right frontal lobe C1 segment Top expressed in granulocyte tibiofemoral joint thymus dentate gyrus of hippocampal formation granule cell stroma of bone marrow lymph node blood spleen mesenteric lymph nodes neural layer of retina More reference expression data BioGPS More reference expression data
Gene ontology Molecular function alpha-1B adrenergic receptor binding 14-3-3 protein binding protein kinase B binding protein binding enzyme binding angiotensin receptor binding molecular adaptor activity signaling receptor binding G protein-coupled receptor binding ubiquitin protein ligase binding identical protein binding arrestin family protein binding protein-containing complex binding protein domain specific binding alpha-1A adrenergic receptor binding type 1 angiotensin receptor binding D1 dopamine receptor binding follicle-stimulating hormone receptor binding type 2A serotonin receptor binding platelet activating factor receptor binding mitogen-activated protein kinase binding Cellular component cytoplasm cytosol postsynaptic membrane postsynaptic density membrane plasma membrane endocytic vesicle dendritic spine intracellular anatomical structure basolateral plasma membrane clathrin-coated pit cytoplasmic vesicle nucleus intracellular membrane-bounded organelle endosome Biological process proteasome-mediated ubiquitin-dependent protein catabolic process positive regulation of calcium ion transport regulation of protein phosphorylation negative regulation of interleukin-1 beta production negative regulation of protein kinase B signaling negative regulation of cysteine-type endopeptidase activity involved in apoptotic process positive regulation of protein kinase B signaling positive regulation of protein phosphorylation endocytosis regulation of G protein-coupled receptor signaling pathway positive regulation of receptor internalization negative regulation of release of cytochrome c from mitochondria negative regulation of interleukin-6 production receptor internalization transcription by RNA polymerase II positive regulation of peptidyl-serine phosphorylation detection of temperature stimulus involved in sensory perception of pain follicle-stimulating hormone signaling pathway platelet activation dopamine receptor signaling pathway negative regulation of protein ubiquitination brain development negative regulation of GTPase activity negative regulation of toll-like receptor signaling pathway protein ubiquitination positive regulation of DNA biosynthetic process positive regulation of ERK1 and ERK2 cascade positive regulation of peptidyl-tyrosine phosphorylation cell chemotaxis protein transport negative regulation of natural killer cell mediated cytotoxicity regulation of androgen receptor signaling pathway positive regulation of synaptic transmission, dopaminergic negative regulation of tumor necrosis factor production negative regulation of signal transduction positive regulation of protein ubiquitination transforming growth factor beta receptor signaling pathway negative regulation of NF-kappaB transcription factor activity negative regulation of smooth muscle cell apoptotic process desensitization of G protein-coupled receptor signaling pathway by arrestin signal transduction adult walking behavior negative regulation of interleukin-12 production Wnt signaling pathway, planar cell polarity pathway negative regulation of protein phosphorylation G protein-coupled receptor internalization positive regulation of gene expression protein deubiquitination membrane organization positive regulation of cardiac muscle cell differentiation G protein-coupled receptor signaling pathway excitatory postsynaptic potential positive regulation of collagen biosynthetic process negative regulation of neuron apoptotic process positive regulation of epithelial cell apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 409 216869 Ensembl ENSG00000141480 ENSMUSG00000060216 UniProt P32121 Q91YI4 RefSeq (mRNA) NM_001257328 NM_001257329 NM_001257330 NM_001257331 NM_004313 NM_199004 NM_001330064 NM_001271358 NM_001271359 NM_001271360 NM_145429 RefSeq (protein) NP_001244257 NP_001244258 NP_001244259 NP_001244260 NP_001316993 NP_004304 NP_945355 NP_001258287 NP_001258288 NP_001258289 NP_663404 Location (UCSC) Chr 17: 4.71 – 4.72 Mb Chr 11: 70.32 – 70.33 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Beta-arrestin-2, or β-arrestin2, 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, as well as having signalling roles in their own right. 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.

The protein may interact with the agonist DOI in 5-HT_2A receptor signaling.

Arrestin beta 2 is crucial for the development of tolerance to morphine and other opioids.

Interactions

Arrestin beta 2 has been shown to interact with

• AP2B1,
• PSCD2,
• Mdm2, and
• RALGDS.

Further reading

• Lefkowitz RJ (July 1998). "G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization". The Journal of Biological Chemistry. 273 (30): 18677–80. doi:10.1074/jbc.273.30.18677. PMID 9668034.
• Attramadal H, Arriza JL, Aoki C, Dawson TM, Codina J, Kwatra MM, Snyder SH, Caron MG, Lefkowitz RJ (September 1992). "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family". The Journal of Biological Chemistry. 267 (25): 17882–90. doi:10.1016/S0021-9258(19)37125-X. PMID 1517224.
• Rapoport B, Kaufman KD, Chazenbalk GD (April 1992). "Cloning of a member of the arrestin family from a human thyroid cDNA library". Molecular and Cellular Endocrinology. 84 (3): R39-43. doi:10.1016/0303-7207(92)90038-8. PMID 1587386. S2CID 1964362.
• Calabrese G, Sallese M, Stornaiuolo A, Stuppia L, Palka G, De Blasi A (September 1994). "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, Ambrosini G, Masini M, Rotilio D, De Blasi A (May 1993). "Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing". The Journal of Biological Chemistry. 268 (13): 9753–61. doi:10.1016/S0021-9258(18)98412-7. PMID 8486659.
• Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J (February 1997). "Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor". FEBS Letters. 402 (2–3): 203–8. Bibcode:1997FEBSL.402..203L. doi:10.1016/S0014-5793(96)01531-1. PMID 9037196. S2CID 21074692.
• Barak LS, Ferguson SS, Zhang J, Caron MG (October 1997). "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation". The Journal of Biological Chemistry. 272 (44): 27497–500. doi:10.1074/jbc.272.44.27497. PMID 9346876.
• Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS (March 1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proceedings of the National Academy of Sciences of the United States of America. 96 (7): 3712–7. Bibcode:1999PNAS...96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
• Cheng ZJ, Zhao J, Sun Y, Hu W, Wu YL, Cen B, Wu GX, Pei G (January 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". The Journal of Biological Chemistry. 275 (4): 2479–85. doi:10.1074/jbc.275.4.2479. PMID 10644702.
• Lin F, Wang Hy, Malbon CC (June 2000). "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". The Journal of Biological Chemistry. 275 (25): 19025–34. doi:10.1074/jbc.275.25.19025. PMID 10858453.
• McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ (November 2000). "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science. 290 (5496): 1574–7. Bibcode:2000Sci...290.1574M. doi:10.1126/science.290.5496.1574. PMID 11090355.
• Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ (February 2001). "Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds". Proceedings of the National Academy of Sciences of the United States of America. 98 (5): 2449–54. Bibcode:2001PNAS...98.2449L. doi:10.1073/pnas.041604898. PMC 30158. PMID 11226259.
• Cen B, Yu Q, Guo J, Wu Y, Ling K, Cheng Z, Ma L, Pei G (March 2001). "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". Journal of Neurochemistry. 76 (6): 1887–94. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507. S2CID 83485138.
• Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG (June 2001). "Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*". The Journal of Biological Chemistry. 276 (22): 19452–60. doi:10.1074/jbc.M101450200. PMID 11279203.
• Miller WE, McDonald PH, Cai SF, Field ME, Davis RJ, Lefkowitz RJ (July 2001). "Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3". The Journal of Biological Chemistry. 276 (30): 27770–7. doi:10.1074/jbc.M102264200. PMID 11356842.
• 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". The Journal of Biological Chemistry. 276 (45): 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.
• Hilairet S, Bélanger C, Bertrand J, Laperrière A, Foord SM, Bouvier M (November 2001). "Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin". The Journal of Biological Chemistry. 276 (45): 42182–90. doi:10.1074/jbc.M107323200. PMID 11535606.
• Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ (November 2001). "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin". Science. 294 (5545): 1307–13. Bibcode:2001Sci...294.1307S. doi:10.1126/science.1063866. PMID 11588219. S2CID 23486946.
• Chen Z, Dupré DJ, Le Gouill C, Rola-Pleszczynski M, Stanková J (March 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". The Journal of Biological Chemistry. 277 (9): 7356–62. doi:10.1074/jbc.M110058200. PMID 11729201.

External links

• Human ARRB2 genome location and ARRB2 gene details page in the UCSC Genome Browser.

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