Arrestin beta 2 information

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)
End	4,721,499 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	70,331,654 bp
RNA expression pattern
	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
	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
	409
	216869
	ENSG00000141480
	ENSMUSG00000060216
	P32121
	Q91YI4
NM_001257328; NM_001257329; NM_001257330; NM_001257331; NM_004313;
	NM_199004; NM_001330064
	NM_001271358; NM_001271359; NM_001271360; NM_145429
NP_001244257; NP_001244258; NP_001244259; NP_001244260; NP_001316993;
	NP_004304; NP_945355
	NP_001258287; NP_001258288; NP_001258289; NP_663404
	Wikidata
View/Edit Human	View/Edit Mouse

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,^[5]^[6]^[7] as well as having signalling roles in their own right.^[8]^[9]^[10]^[11]^[12] 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.^[13]

The protein may interact with the agonist DOI in 5-HT_2A receptor signaling.^[14]^[15]

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000141480 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000060216 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK (July 2008). "Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice". Behavioural Pharmacology. 19 (4): 298–307. doi:10.1097/FBP.0b013e328308f1e6. PMC 2751575. PMID 18622177.
^ 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-arrestin2 expression in mice periaqueductal gray matter". International Journal of Molecular Sciences. 10 (3): 954–63. doi:10.3390/ijms10030954. PMC 2672012. PMID 19399231.
^ Zheng H, Loh HH, Law PY (January 2008). "Beta-arrestin-dependent mu-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.
^ 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). "Beta-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.
^ Barki-Harrington L, Rockman HA (February 2008). "Beta-arrestins: multifunctional cellular mediators". Physiology. 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.
^ "ARRB2 arrestin beta 2 [ Homo sapiens (human) ]". National Center for Biotechnology Information.
^ Schmid CL, Raehal KM, Bohn LM (January 2008). "Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo". Proceedings of the National Academy of Sciences of the United States of America. 105 (3): 1079–84. doi:10.1073/pnas.0708862105. PMC 2242710. PMID 18195357.
^ Abbas A, Roth BL (January 2008). "Arresting serotonin". Proceedings of the National Academy of Sciences of the United States of America. 105 (3): 831–2. Bibcode:2008PNAS..105..831A. doi:10.1073/pnas.0711335105. PMC 2242676. PMID 18195368.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000141480 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000060216 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid18622177-5] Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK (July 2008). "Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice". Behavioural Pharmacology. 19 (4): 298–307. doi:10.1097/FBP.0b013e328308f1e6. PMC 2751575. PMID 18622177.

[pmid19399231-6] 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-arrestin2 expression in mice periaqueductal gray matter". International Journal of Molecular Sciences. 10 (3): 954–63. doi:10.3390/ijms10030954. PMC 2672012. PMID 19399231.

[pmid17947509-7] Zheng H, Loh HH, Law PY (January 2008). "Beta-arrestin-dependent mu-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.

[pmid17215450-8] 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.

[pmid18037927-9] Defea K (March 2008). "Beta-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.

[pmid18268361-10] Barki-Harrington L, Rockman HA (February 2008). "Beta-arrestins: multifunctional cellular mediators". Physiology. 23: 17–22. doi:10.1152/physiol.00042.2007. PMID 18268361.

[pmid19103204-11] 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.

[pmid19442183-12] 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.

[13] "ARRB2 arrestin beta 2 [ Homo sapiens (human) ]". National Center for Biotechnology Information.

[pmid18195357-14] Schmid CL, Raehal KM, Bohn LM (January 2008). "Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo". Proceedings of the National Academy of Sciences of the United States of America. 105 (3): 1079–84. doi:10.1073/pnas.0708862105. PMC 2242710. PMID 18195357.

[pmid18195368-15] Abbas A, Roth BL (January 2008). "Arresting serotonin". Proceedings of the National Academy of Sciences of the United States of America. 105 (3): 831–2. Bibcode:2008PNAS..105..831A. doi:10.1073/pnas.0711335105. PMC 2242676. PMID 18195368.

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