Arrestin beta 1

Arrestin, beta 1, also known as ARRB1, is a human gene. [cite web | title = Entrez Gene: ARRB1 arrestin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=408| accessdate = ]

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summary_text = 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. [cite web | title = Entrez Gene: ARRB1 arrestin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=408| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lefkowitz RJ |title=G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18677–80 |year= 1998 |pmid= 9668034 |doi=
*cite journal | author=Lohse MJ, Benovic JL, Codina J, "et al." |title=beta-Arrestin: a protein that regulates beta-adrenergic receptor function. |journal=Science |volume=248 |issue= 4962 |pages= 1547–50 |year= 1990 |pmid= 2163110 |doi=
*cite journal | author=Calabrese G, Sallese M, Stornaiuolo A, "et al." |title=Assignment of the beta-arrestin 1 gene (ARRB1) to human chromosome 11q13. |journal=Genomics |volume=24 |issue= 1 |pages= 169–71 |year= 1995 |pmid= 7896272 |doi= 10.1006/geno.1994.1594
*cite journal | author=Parruti G, Peracchia F, Sallese M, "et al." |title=Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9753–61 |year= 1993 |pmid= 8486659 |doi=
*cite journal | author=Iacovelli L, Franchetti R, Masini M, De Blasi A |title=GRK2 and beta-arrestin 1 as negative regulators of thyrotropin receptor-stimulated response. |journal=Mol. Endocrinol. |volume=10 |issue= 9 |pages= 1138–46 |year= 1997 |pmid= 8885248 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Goodman OB, Krupnick JG, Gurevich VV, "et al." |title=Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 15017–22 |year= 1997 |pmid= 9169477 |doi=
*cite journal | author=Lin FT, Krueger KM, Kendall HE, "et al." |title=Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 31051–7 |year= 1998 |pmid= 9388255 |doi=
*cite journal | author=Aragay AM, Mellado M, Frade JM, "et al." |title=Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 6 |pages= 2985–90 |year= 1998 |pmid= 9501202 |doi=
*cite journal | author=ter Haar E, Musacchio A, Harrison SC, Kirchhausen T |title=Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. |journal=Cell |volume=95 |issue= 4 |pages= 563–73 |year= 1998 |pmid= 9827808 |doi=
*cite journal | author=Luttrell LM, Ferguson SS, Daaka Y, "et al." |title=Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. |journal=Science |volume=283 |issue= 5402 |pages= 655–61 |year= 1999 |pmid= 9924018 |doi=
*cite journal | author=McDonald PH, Cote NL, Lin FT, "et al." |title=Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation. |journal=J. Biol. Chem. |volume=274 |issue= 16 |pages= 10677–80 |year= 1999 |pmid= 10196135 |doi=
*cite journal | author=Lin FT, Miller WE, Luttrell LM, Lefkowitz RJ |title=Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 15971–4 |year= 1999 |pmid= 10347142 |doi=
*cite journal | author=McConalogue K, Déry O, Lovett M, "et al." |title=Substance P-induced trafficking of beta-arrestins. The role of beta-arrestins in endocytosis of the neurokinin-1 receptor. |journal=J. Biol. Chem. |volume=274 |issue= 23 |pages= 16257–68 |year= 1999 |pmid= 10347182 |doi=
*cite journal | author=Miller WE, Maudsley S, Ahn S, "et al." |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 15 |pages= 11312–9 |year= 2000 |pmid= 10753943 |doi=
*cite journal | author=Laporte SA, Oakley RH, Holt JA, "et al." |title=The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits. |journal=J. Biol. Chem. |volume=275 |issue= 30 |pages= 23120–6 |year= 2000 |pmid= 10770944 |doi= 10.1074/jbc.M002581200
*cite journal | author=Bennett TA, Maestas DC, Prossnitz ER |title=Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24590–4 |year= 2000 |pmid= 10823817 |doi= 10.1074/jbc.C000314200
*cite journal | author=Shiina T, Kawasaki A, Nagao T, Kurose H |title=Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors. |journal=J. Biol. Chem. |volume=275 |issue= 37 |pages= 29082–90 |year= 2000 |pmid= 10862778 |doi= 10.1074/jbc.M909757199
*cite journal | author=Barlic J, Andrews JD, Kelvin AA, "et al." |title=Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI. |journal=Nat. Immunol. |volume=1 |issue= 3 |pages= 227–33 |year= 2001 |pmid= 10973280 |doi= 10.1038/79767

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