Human protein and coding gene
ARRB1 |
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Available structures |
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PDB | Ortholog search: PDBe RCSB |
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Identifiers |
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Aliases | ARRB1, ARB1, ARR1, Arrestin beta 1 |
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External IDs | OMIM: 107940; MGI: 99473; HomoloGene: 2981; GeneCards: ARRB1; OMA:ARRB1 - orthologs |
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Gene location (Human) |
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| Chr. | Chromosome 11 (human)[1] |
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| Band | 11q13.4 | Start | 75,260,122 bp[1] |
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End | 75,351,705 bp[1] |
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Gene location (Mouse) |
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| Chr. | Chromosome 7 (mouse)[2] |
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| Band | 7 E1|7 54.09 cM | Start | 99,184,673 bp[2] |
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End | 99,255,978 bp[2] |
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RNA expression pattern |
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Bgee | Human | Mouse (ortholog) |
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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
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| Top expressed in | - fetal liver hematopoietic progenitor cell
- superior frontal gyrus
- inferior colliculus
- granulocyte
- molar
- tibiofemoral joint
- superior colliculus
- dentate gyrus of hippocampal formation granule cell
- primary visual cortex
- cerebellar cortex
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| More reference expression data |
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BioGPS | | More reference expression data |
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Gene ontology |
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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 |
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Wikidata |
View/Edit Human | View/Edit Mouse |
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Arrestin, beta 1, also known as ARRB1, is a protein which in humans is encoded by the ARRB1 gene.[5][6]
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 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.[7]
Interactions
Arrestin beta 1 has been shown to interact with
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000137486 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000018909 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ 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.
- ^ a b "Entrez Gene: ARRB1 arrestin, beta 1".
- ^ Peterson YK, Luttrell LM (July 2017). "The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling". Pharmacological Reviews. 69 (3): 256–297. doi:10.1124/pr.116.013367. PMC 5482185. PMID 28626043.
- ^ a b 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". The Journal of Biological Chemistry. 276 (45): 42509–42513. doi:10.1074/jbc.M108399200. PMID 11533043.
- ^ Conlan LA, Martin TJ, Gillespie MT (September 2002). "The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B". FEBS Letters. 527 (1–3): 71–75. doi:10.1016/S0014-5793(02)03164-2. PMID 12220636. S2CID 83640616.
- ^ 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". Proceedings of the National Academy of Sciences of the United States of America. 98 (26): 14889–14894. Bibcode:2001PNAS...9814889C. doi:10.1073/pnas.211572798. PMC 64954. PMID 11742073.
- ^ 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". The Journal of Biological Chemistry. 278 (13): 11648–11653. doi:10.1074/jbc.M208109200. PMID 12538596.
- ^ 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". The Journal of Biological Chemistry. 283 (32): 22166–22176. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533.
- ^ Cen B, Yu Q, Guo J, Wu Y, Ling K, Cheng Z, et al. (March 2001). "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". Journal of Neurochemistry. 76 (6): 1887–1894. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507. S2CID 83485138.
- ^ Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, et al. (August 2002). "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nature Cell Biology. 4 (8): 547–555. doi:10.1038/ncb821. PMID 12105416. S2CID 20784208.
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 behavor 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
PDB gallery
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1g4m: CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1 -
1g4r: CRYSTAL STRUCTURE OF BOVINE BETA-ARRESTIN 1 -
1jsy: Crystal structure of bovine arrestin-2 -
1zsh: Crystal structure of bovine arrestin-2 in complex with inositol hexakisphosphate (IP6) |