Arrestin beta 1

Arrestin, beta 1

PDB rendering based on 1g4m.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2IV8

Identifiers

Symbols

ARRB1 ; ARB1; ARR1

External IDs

OMIM: 107940 MGI: 99473 HomoloGene: 2981 ChEMBL: 1795088 GeneCards: ARRB1 Gene

Gene ontology
Molecular function	• histone acetyltransferase activity • enzyme inhibitor activity • GTPase activator activity • insulin-like growth factor receptor binding • protein binding • transcription factor binding • estrogen receptor binding • mitogen-activated protein kinase kinase binding • ubiquitin protein ligase binding • alpha-1A adrenergic receptor binding • alpha-1B adrenergic receptor binding • angiotensin receptor binding • follicle-stimulating hormone receptor binding • V2 vasopressin receptor binding • AP-2 adaptor complex binding • clathrin adaptor activity • cysteine-type endopeptidase inhibitor activity involved in apoptotic process • transcription regulatory region DNA binding • ion channel binding • protein phosphorylated amino acid binding
Cellular component	• Golgi membrane • chromatin • nucleus • nucleoplasm • cytoplasm • lysosomal membrane • cytosol • heterotrimeric G-protein complex • plasma membrane • coated pit • postsynaptic density • basolateral plasma membrane • cytoplasmic vesicle membrane • pseudopodium • cytoplasmic vesicle • dendritic spine • postsynaptic membrane
Biological process	• activation of MAPK activity • positive regulation of protein phosphorylation • G-protein coupled receptor internalization • positive regulation of receptor internalization • transcription from RNA polymerase II promoter • post-Golgi vesicle-mediated transport • Notch signaling pathway • blood coagulation • phototransduction • protein transport • protein ubiquitination • platelet activation • negative regulation of protein ubiquitination • positive regulation of protein ubiquitination • negative regulation of NF-kappaB transcription factor activity • positive regulation of protein binding • negative regulation of interleukin-6 production • negative regulation of interleukin-8 production • positive regulation of peptidyl-serine phosphorylation • negative regulation of GTPase activity • positive regulation of smooth muscle cell apoptotic process • positive regulation of Rho protein signal transduction • positive regulation of histone acetylation • positive regulation of insulin secretion involved in cellular response to glucose stimulus • follicle-stimulating hormone signaling pathway • stress fiber assembly • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process • proteasome-mediated ubiquitin-dependent protein catabolic process • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process • positive regulation of GTPase activity • positive regulation of transcription from RNA polymerase II promoter • membrane organization • negative regulation of ERK1 and ERK2 cascade • positive regulation of ERK1 and ERK2 cascade • positive regulation of histone H4 acetylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

408

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
75.26 – 75.35 Mb

Chr 7:
99.54 – 99.61 Mb

PubMed search

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

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

Arrestin beta 1 has been shown to interact with

References

↑ 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.
1 2 "Entrez Gene: ARRB1 arrestin, beta 1".
1 2 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.
↑ 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.

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.

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: 218–22. doi:10.1038/nature13430. PMID 25043026.

PDB gallery

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)

Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton)

Arrestin	SAG ARRB1 ARRB2 ARR3

Membrane-spanning 4A	MS4A1 MS4A2 MS4A3 MS4A4A MS4A4E MS4A5 MS4A6A MS4A6E MS4A7 MS4A8B MS4A9 MS4A10 MS4A12 MS4A13 MS4A14 MS4A15 MS4A18

Myelin	Myelin basic protein PMP2 Myelin proteolipid protein PLP1 Myelin oligodendrocyte glycoprotein Myelin-associated glycoprotein Myelin protein zero

Pulmonary surfactant	Pulmonary surfactant-associated protein B Pulmonary surfactant-associated protein C

Tetraspanin	TSPAN1 TSPAN2 TSPAN3 TSPAN4 TSPAN5 TSPAN6 TSPAN7 TSPAN8 TSPAN9 TSPAN10 TSPAN11 TSPAN12 TSPAN13 TSPAN14 TSPAN15 TSPAN16 TSPAN17 TSPAN18 TSPAN19 TSPAN20 TSPAN21 TSPAN22 TSPAN23 TSPAN24 TSPAN25 TSPAN26 TSPAN27 TSPAN28 TSPAN29 TSPAN30 TSPAN31 TSPAN32 TSPAN33 TSPAN34

Other/ungrouped	Calnexin LDL-receptor-related protein-associated protein Neurofibromin 2 Presenilin PSEN1 PSEN2 HFE Phospholipid transfer proteins Dysferlin STRC OTOF

see also other cell membrane protein disorders

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Arrestin beta 1

Function

Interactions

References

Further reading