Arrestin beta 1

From Wikipedia, the free encyclopedia

Arrestin, beta 1

PDB rendering based on 1g4m.

Available structures: 1g4m, 1g4r, 1jsy, 1zsh

Identifiers

Symbol(s)

ARRB1; ARB1; ARR1

External IDs

OMIM: 107940 MGI: 99473 HomoloGene: 2981

Gene ontology
Molecular Function:	• enzyme inhibitor activity • protein binding
Cellular Component:	• intracellular • membrane fraction • soluble fraction • cytoplasm • heterotrimeric G-protein complex • plasma membrane
Biological Process:	• signal transduction • sensory perception • regulation of G-protein coupled receptor protein signaling pathway • response to stimulus

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004041 (mRNA)
NP_004032 (protein)

NM_177231 (mRNA)
NP_796205 (protein)

Location

Chr 11: 74.65 - 74.74 Mb

Chr 7: 99.41 - 99.48 Mb

Pubmed search

[1]

[2]

Arrestin, beta 1, also known as ARRB1, is a human gene.^[1]

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]

[edit] References

[edit] 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. 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. 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. PMID 8885248.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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.