Arrestin beta 1

Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.[5][6]

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
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11q13.4 Start 75,260,122 bp[1] End 75,351,705 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7 E1|7 54.09 cM Start 99,535,466 bp[2] End 99,606,771 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0005097, GO:0005099, GO:0005100 GTPase activator activity • histone acetyltransferase activity • GO:0048551 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 • GO:0001948 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 • receptor binding • enzyme binding • estrogen receptor binding • alpha-1A adrenergic receptor binding • follicle-stimulating hormone receptor binding • ion channel binding • clathrin binding • G-protein coupled receptor binding Cellular component • cytoplasm • cytosol • postsynaptic membrane • membrane • cell nucleus • cell projection • dendritic spine • heterotrimeric G-protein complex • chromatin • cell membrane • intracellular • nucleoplasm • clathrin-coated pit • pseudopodia • GO:0097483, GO:0097481 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 protein signaling pathway • positive regulation of receptor internalization • transcription from RNA polymerase II promoter • stress fiber assembly • follicle-stimulating hormone signaling pathway • platelet activation • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process • GO:0034259 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 • activation of MAPK activity • 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 from RNA polymerase II promoter • signal transduction • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • apoptotic process • response to drug • 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 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: 99.54 – 99.61 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6] Beta-arrestin might also play a role as scaffold protein in the GPCR pathways.

Interactions

Arrestin beta 1 has been shown to interact with

• Arf6,[7]
• PTHLH,[8]
• DVL2[9]
• Mdm2,[10][11]
• OPRD1,[12]
• PSCD2,[7] and
• RALGDS.[13]

References

1. GRCh38: Ensembl release 89: ENSG00000137486 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000018909 - 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.
5. 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. PMID 8486659.
6. "Entrez Gene: ARRB1 arrestin, beta 1".
7. 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.
8. Conlan LA, Martin TJ, Gillespie MT (September 2002). "The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B". FEBS Lett. 527 (1–3): 71–5. doi:10.1016/S0014-5793(02)03164-2. PMID 12220636. S2CID 83640616.
9. Chen W, Hu LA, Semenov MV, Yanagawa S, Kikuchi A, Lefkowitz RJ, Miller WE (December 2001). "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 14889–94. doi:10.1073/pnas.211572798. PMC 64954. PMID 11742073.
10. 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.
11. 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 beta2-adrenergic receptor". J. Biol. Chem. 283 (32): 22166–76. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533.
12. 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". J. Neurochem. 76 (6): 1887–94. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507. S2CID 83485138.
13. 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. S2CID 20784208.

Further reading

• 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.
• Lohse MJ, Benovic JL, Codina J, et al. (1990). "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science. 248 (4962): 1547–50. doi:10.1126/science.2163110. PMID 2163110.
• Calabrese G, Sallese M, Stornaiuolo A, et al. (1995). "Assignment of the beta-arrestin 1 gene (ARRB1) to human chromosome 11q13". Genomics. 24 (1): 169–71. doi:10.1006/geno.1994.1594. PMID 7896272.
• 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.
• Iacovelli L, Franchetti R, Masini M, De Blasi A (1997). "GRK2 and beta-arrestin 1 as negative regulators of thyrotropin receptor-stimulated response". Mol. Endocrinol. 10 (9): 1138–46. doi:10.1210/me.10.9.1138. PMID 8885248.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Goodman OB, Krupnick JG, Gurevich VV, et al. (1997). "Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain". J. Biol. Chem. 272 (23): 15017–22. doi:10.1074/jbc.272.23.15017. PMID 9169477.
• Lin FT, Krueger KM, Kendall HE, et al. (1998). "Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1". J. Biol. Chem. 272 (49): 31051–7. doi:10.1074/jbc.272.49.31051. PMID 9388255.
• Aragay AM, Mellado M, Frade JM, et al. (1998). "Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2". Proc. Natl. Acad. Sci. U.S.A. 95 (6): 2985–90. doi:10.1073/pnas.95.6.2985. PMC 19681. PMID 9501202.
• ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker". Cell. 95 (4): 563–73. doi:10.1016/S0092-8674(00)81623-2. PMC 4428171. PMID 9827808.
• Luttrell LM, Ferguson SS, Daaka Y, et al. (1999). "Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes". Science. 283 (5402): 655–61. doi:10.1126/science.283.5402.655. PMID 9924018.
• McDonald PH, Cote NL, Lin FT, et al. (1999). "Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation". J. Biol. Chem. 274 (16): 10677–80. doi:10.1074/jbc.274.16.10677. PMID 10196135.
• Lin FT, Miller WE, Luttrell LM, Lefkowitz RJ (1999). "Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases". J. Biol. Chem. 274 (23): 15971–4. doi:10.1074/jbc.274.23.15971. PMID 10347142.
• McConalogue K, Déry O, Lovett M, et al. (1999). "Substance P-induced trafficking of beta-arrestins. The role of beta-arrestins in endocytosis of the neurokinin-1 receptor". J. Biol. Chem. 274 (23): 16257–68. doi:10.1074/jbc.274.23.16257. PMID 10347182.
• Miller WE, Maudsley S, Ahn S, et al. (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". J. Biol. Chem. 275 (15): 11312–9. doi:10.1074/jbc.275.15.11312. PMID 10753943.
• Laporte SA, Oakley RH, Holt JA, et al. (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". J. Biol. Chem. 275 (30): 23120–6. doi:10.1074/jbc.M002581200. PMID 10770944.
• Bennett TA, Maestas DC, Prossnitz ER (2000). "Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence". J. Biol. Chem. 275 (32): 24590–4. doi:10.1074/jbc.C000314200. PMID 10823817.
• Shiina T, Kawasaki A, Nagao T, Kurose H (2000). "Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors". J. Biol. Chem. 275 (37): 29082–90. doi:10.1074/jbc.M909757199. PMID 10862778.
• Barlic J, Andrews JD, Kelvin AA, et al. (2001). "Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI". Nat. Immunol. 1 (3): 227–33. doi:10.1038/79767. PMID 10973280. S2CID 6151896.

• Shukla, A. K.; Westfield, G. H.; Xiao, K; Reis, R. I.; Huang, L. Y.; Tripathi-Shukla, P; Qian, J; Li, S; Blanc, A; Oleskie, A. N.; Dosey, A. M.; Su, M; Liang, C. R.; Gu, L. L.; Shan, J. M.; Chen, X; Hanna, R; Choi, M; Yao, X. J.; Klink, B. U.; Kahsai, A. W.; Sidhu, S. S.; Koide, S; Penczek, P. A.; Kossiakoff, A. A.; Woods Jr, V. L.; Kobilka, B. K.; Skiniotis, G; Lefkowitz, R. J. (2014). "Visualization of arrestin recruitment by a G-protein-coupled receptor". Nature. 512 (7513): 218–22. doi:10.1038/nature13430. PMC 4134437. PMID 25043026.

External links

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