Arestin beta 1

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Arestin, beta 1

PDB prikaz baziran na 1g4m.
Dostupne strukture
1g4m, 1g4r, 1jsy, 1zsh
Identifikatori
SimboliARRB1; ARB1; ARR1
Vanjski IDOMIM: 107940 MGI: 99473 HomoloGene: 2981 GeneCards: ARRB1 Gene
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez408109689
EnsemblENSG00000137486ENSMUSG00000018909
UniProtP49407Q8BWG8
RefSeq (mRNA)NM_004041NM_177231
RefSeq (protein)NP_004032NP_796205
Lokacija (UCSC)Chr 11:
74.65 - 74.74 Mb		Chr 7:
99.41 - 99.48 Mb
PubMed pretraga[1][2]

Arestin beta 1, ARRB1, je protein koji je čoveka kodiran ARRB1 genom.[1][2]

Funkcije

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Za članove arestin/beta-arestin proteinske familije se smatra da učestvuju u agonistima posredovanoj desenzitizaciji G protein-spregnutih receptora i uzrokuju specifično prigušivanje ćelijskog responsa na stimuluse kao što su hormoni, neurotransmitera, ili senzorski signali. Arrestin beta 1 je citosolni protein koji deluje kao kofaktor u beta-adrenergičkom receptorskom kinazom (BARK) posredovanoj desenzitizaciji beta-adrenergičkog receptora. Pored centralnog nervnog sistema, on je izražen u visokim nivoima u perifernim krvnim leukocitima, i stoga se za BARK/beta-arestinski sistem da ima značajnu ulogu u regulaciji receptorom-posredovanih imunskih funkcija. Alternativno splajsovani transkripti kodiraju različite izoforme arestina beta 1. One su bile opisane, međutim, njihove precizne funkcije nisu poznate.[2]

Interakcije

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Za arestin beta 1 je bilo pokazano da interaguje sa delta opioidnim receptorom,[3] Arf6,[4] paratiroidnom hormonu srodnim proteinom,[5] RALGDS,[6] PSCD2,[4] DVL2[7] i Mdm2.[8][9]

Reference

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  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. Arhivirano iz originala na datum 2005-01-03. Pristupljeno 2014-05-10. 
  2. ↑ 2,0 2,1 „Entrez Gene: ARRB1 arrestin, beta 1”. 
  3. ↑ 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. (United States) 76 (6): 1887–94. DOI:10.1046/j.1471-4159.2001.00204.x. ISSN 0022-3042. PMID 11259507. 
  4. ↑ 4,0 4,1 Claing, A; Chen W, Miller W E, Vitale N, Moss J, Premont R T, Lefkowitz R J (November 2001). „beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis”. J. Biol. Chem. (United States) 276 (45): 42509–13. DOI:10.1074/jbc.M108399200. ISSN 0021-9258. PMID 11533043. 
  5. ↑ Conlan, Lindus A; Martin T John, Gillespie Matthew T (September 2002). „The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B”. FEBS Lett. (Netherlands) 527 (1-3): 71–5. DOI:10.1016/S0014-5793(02)03164-2. ISSN 0014-5793. PMID 12220636. 
  6. ↑ Bhattacharya, Moshmi; Anborgh Pieter H, Babwah Andy V, Dale Lianne B, Dobransky Tomas, Benovic Jeffery L, Feldman Ross D, Verdi Joseph M, Rylett R Jane, Ferguson Stephen S G (August 2002). „Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization”. Nat. Cell Biol. (England) 4 (8): 547–55. DOI:10.1038/ncb821. ISSN 1465-7392. PMID 12105416. 
  7. ↑ Chen, W; Hu L A, Semenov M V, Yanagawa S, Kikuchi A, Lefkowitz R J, Miller W E (December 2001). „beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins”. Proc. Natl. Acad. Sci. U.S.A. (United States) 98 (26): 14889–94. DOI:10.1073/pnas.211572798. ISSN 0027-8424. PMC 64954. PMID 11742073. 
  8. ↑ Wang, Ping; Wu Yalan, Ge Xin, Ma Lan, Pei Gang (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. (United States) 278 (13): 11648–53. DOI:10.1074/jbc.M208109200. ISSN 0021-9258. PMID 12538596. 
  9. ↑ Shenoy, Sudha K; Xiao Kunhong, Venkataramanan Vidya, Snyder Peter M, Freedman Neil J, Weissman Allan M (August 2008). „Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor”. J. Biol. Chem. (United States) 283 (32): 22166–76. DOI:10.1074/jbc.M709668200. ISSN 0021-9258. PMC 2494938. PMID 18544533. 

Literatura

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  • 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.