Arrestin beta 1

Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.

ARRB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2IV8
Identifiers
Aliases	ARRB1, ARB1, ARR1, Arrestin beta 1
External IDs	OMIM: 107940; MGI: 99473; HomoloGene: 2981; GeneCards: ARRB1; OMA:ARRB1 - orthologs
Gene location (Human) Chr. Chromosome 11 (human) Band 11q13.4 Start 75,260,122 bp End 75,351,705 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 E1|7 54.09 cM Start 99,184,673 bp End 99,255,978 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte granulocyte right lung upper lobe of left lung anterior cingulate cortex sural nerve right frontal lobe prefrontal cortex nucleus accumbens body of stomach Top expressed in fetal liver hematopoietic progenitor cell superior frontal gyrus inferior colliculi granulocyte molar tibiofemoral joint superior colliculus dentate gyrus of hippocampal formation granule cell primary visual cortex cerebellar cortex More reference expression data BioGPS More reference expression data
Gene ontology Molecular function GTPase activator activity histone acetyltransferase activity enzyme inhibitor activity insulin-like growth factor receptor binding transcription factor binding mitogen-activated protein kinase kinase binding clathrin adaptor activity protein phosphorylated amino acid binding cysteine-type endopeptidase inhibitor activity involved in apoptotic process protein binding AP-2 adaptor complex binding alpha-1B adrenergic receptor binding V2 vasopressin receptor binding phosphoprotein binding angiotensin receptor binding ubiquitin protein ligase binding arrestin family protein binding signaling receptor binding enzyme binding estrogen receptor binding alpha-1A adrenergic receptor binding follicle-stimulating hormone receptor binding transmembrane transporter binding clathrin binding G protein-coupled receptor binding Cellular component cytoplasm cytosol postsynaptic membrane membrane nucleus cell projection dendritic spine heterotrimeric G-protein complex chromatin plasma membrane intracellular anatomical structure nucleoplasm clathrin-coated pit pseudopodium postsynaptic density Golgi membrane lysosomal membrane basolateral plasma membrane cytoplasmic vesicle membrane cytoplasmic vesicle nuclear body endosome Biological process positive regulation of Rho protein signal transduction regulation of G protein-coupled receptor signaling pathway positive regulation of receptor internalization transcription by RNA polymerase II stress fiber assembly follicle-stimulating hormone signaling pathway platelet activation positive regulation of cysteine-type endopeptidase activity involved in apoptotic process negative regulation of GTPase activity positive regulation of ERK1 and ERK2 cascade positive regulation of insulin secretion involved in cellular response to glucose stimulus proteasome-mediated ubiquitin-dependent protein catabolic process phototransduction regulation of transcription, DNA-templated transcription, DNA-templated positive regulation of peptidyl-serine phosphorylation negative regulation of interleukin-8 production protein ubiquitination protein transport negative regulation of protein phosphorylation positive regulation of smooth muscle cell apoptotic process positive regulation of histone H4 acetylation positive regulation of protein binding negative regulation of NF-kappaB transcription factor activity positive regulation of protein ubiquitination G protein-coupled receptor internalization negative regulation of cysteine-type endopeptidase activity involved in apoptotic process endocytosis negative regulation of interleukin-6 production positive regulation of histone acetylation negative regulation of protein ubiquitination negative regulation of ERK1 and ERK2 cascade negative regulation of signal transduction positive regulation of transcription by RNA polymerase II signal transduction positive regulation of GTPase activity apoptotic process membrane organization regulation of apoptotic process ubiquitin-dependent protein catabolic process negative regulation of Notch signaling pathway G protein-coupled receptor signaling pathway positive regulation of protein phosphorylation positive regulation of cell population proliferation negative regulation of apoptotic process negative regulation of neuron apoptotic process histone acetylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 408 109689 Ensembl ENSG00000137486 ENSMUSG00000018909 UniProt P49407 Q8BWG8 RefSeq (mRNA) NM_004041 NM_020251 NM_177231 NM_178220 RefSeq (protein) NP_004032 NP_064647 NP_796205 NP_835738 Location (UCSC) Chr 11: 75.26 – 75.35 Mb Chr 7: 99.18 – 99.26 Mb PubMed search
Wikidata
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Function

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 1 is a cytosolic protein and acts as a cofactor in the beta-adrenergic receptor kinase (BARK) mediated desensitization of beta-adrenergic receptors. Besides the central nervous system, it is expressed at high levels in peripheral blood leukocytes, and thus the BARK/beta-arrestin system is believed to play a major role in regulating receptor-mediated immune functions. Alternatively spliced transcripts encoding different isoforms of arrestin beta 1 have been described, however, their exact functions are not known. Beta-arrestin has been shown to play a role as a scaffold that binds intermediates and may direct G-protein signaling by connecting receptors to clathrin-mediated endocytosis.

Interactions

Arrestin beta 1 has been shown to interact with

• Arf6,
• PTHLH,
• DVL2
• Mdm2,
• OPRD1,
• PSCD2, 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): 18677–18680. doi:10.1074/jbc.273.30.18677. PMID 9668034.
• Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ (June 1990). "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science. 248 (4962): 1547–1550. Bibcode:1990Sci...248.1547L. doi:10.1126/science.2163110. PMID 2163110.
• Calabrese G, Sallese M, Stornaiuolo A, Morizio E, Palka G, De Blasi A (November 1994). "Assignment of the beta-arrestin 1 gene (ARRB1) to human chromosome 11q13". Genomics. 24 (1): 169–171. doi:10.1006/geno.1994.1594. PMID 7896272.
• 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): 9753–9761. doi:10.1016/S0021-9258(18)98412-7. PMID 8486659.
• Iacovelli L, Franchetti R, Masini M, De Blasi A (September 1996). "GRK2 and beta-arrestin 1 as negative regulators of thyrotropin receptor-stimulated response". Molecular Endocrinology. 10 (9): 1138–1146. doi:10.1210/mend.10.9.8885248. PMID 8885248.
• Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Goodman OB, Krupnick JG, Gurevich VV, Benovic JL, Keen JH (June 1997). "Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain". The Journal of Biological Chemistry. 272 (23): 15017–15022. doi:10.1074/jbc.272.23.15017. PMID 9169477.
• Lin FT, Krueger KM, Kendall HE, Daaka Y, Fredericks ZL, Pitcher JA, Lefkowitz RJ (December 1997). "Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1". The Journal of Biological Chemistry. 272 (49): 31051–31057. doi:10.1074/jbc.272.49.31051. PMID 9388255.
• Aragay AM, Mellado M, Frade JM, Martin AM, Jimenez-Sainz MC, Martinez-A C, Mayor F (March 1998). "Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2". Proceedings of the National Academy of Sciences of the United States of America. 95 (6): 2985–2990. Bibcode:1998PNAS...95.2985A. doi:10.1073/pnas.95.6.2985. PMC 19681. PMID 9501202.
• ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (November 1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker". Cell. 95 (4): 563–573. doi:10.1016/S0092-8674(00)81623-2. PMC 4428171. PMID 9827808.
• Luttrell LM, Ferguson SS, Daaka Y, Miller WE, Maudsley S, Della Rocca GJ, et al. (January 1999). "Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes". Science. 283 (5402): 655–661. doi:10.1126/science.283.5402.655. PMID 9924018.
• McDonald PH, Cote NL, Lin FT, Premont RT, Pitcher JA, Lefkowitz RJ (April 1999). "Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation". The Journal of Biological Chemistry. 274 (16): 10677–10680. doi:10.1074/jbc.274.16.10677. PMID 10196135.
• Lin FT, Miller WE, Luttrell LM, Lefkowitz RJ (June 1999). "Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases". The Journal of Biological Chemistry. 274 (23): 15971–15974. doi:10.1074/jbc.274.23.15971. PMID 10347142.
• McConalogue K, Déry O, Lovett M, Wong H, Walsh JH, Grady EF, Bunnett NW (June 1999). "Substance P-induced trafficking of beta-arrestins. The role of beta-arrestins in endocytosis of the neurokinin-1 receptor". The Journal of Biological Chemistry. 274 (23): 16257–16268. doi:10.1074/jbc.274.23.16257. PMID 10347182.
• Miller WE, Maudsley S, Ahn S, Khan KD, Luttrell LM, Lefkowitz RJ (April 2000). "beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis". The Journal of Biological Chemistry. 275 (15): 11312–11319. doi:10.1074/jbc.275.15.11312. PMID 10753943.
• Laporte SA, Oakley RH, Holt JA, Barak LS, Caron MG (July 2000). "The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits". The Journal of Biological Chemistry. 275 (30): 23120–23126. doi:10.1074/jbc.M002581200. PMID 10770944.
• Bennett TA, Maestas DC, Prossnitz ER (August 2000). "Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence". The Journal of Biological Chemistry. 275 (32): 24590–24594. doi:10.1074/jbc.C000314200. PMID 10823817.
• Shiina T, Kawasaki A, Nagao T, Kurose H (September 2000). "Interaction with beta-arrestin determines the difference in internalization behavior between beta1- and beta2-adrenergic receptors". The Journal of Biological Chemistry. 275 (37): 29082–29090. doi:10.1074/jbc.M909757199. PMID 10862778.
• Barlic J, Andrews JD, Kelvin AA, Bosinger SE, DeVries ME, Xu L, et al. (September 2000). "Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI". Nature Immunology. 1 (3): 227–233. doi:10.1038/79767. PMID 10973280. S2CID 6151896.
• Shukla AK, Westfield GH, Xiao K, Reis RI, Huang LY, Tripathi-Shukla P, et al. (August 2014). "Visualization of arrestin recruitment by a G-protein-coupled receptor". Nature. 512 (7513): 218–222. Bibcode:2014Natur.512..218S. doi:10.1038/nature13430. PMC 4134437. PMID 25043026.

External links

• Human ARRB1 genome location and ARRB1 gene details page in the UCSC Genome Browser.