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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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Arrestin beta 1

Introduction

Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.[1][2]

Function

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

Interactions

Interactions

Arrestin beta 1 has been shown to interact with

References

References

  1. ↑ 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.
  2. ↑ 2.0 2.1 “Entrez Gene: ARRB1 arrestin, beta 1”.
  3. ↑ 3.0 3.1 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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.
  9. ↑ 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.
Further reading

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. 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.
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