Arrestin beta 1

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Arrestin, beta 1
Protein ARRB1 PDB 1g4m.png
PDB rendering based on 1g4m.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ARRB1 ; ARB1; ARR1
External IDs OMIM107940 MGI99473 HomoloGene2981 ChEMBL: 1795088 GeneCards: ARRB1 Gene
RNA expression pattern
PBB GE ARRB1 218832 x at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 408 109689
Ensembl ENSG00000137486 ENSMUSG00000018909
UniProt P49407 Q8BWG8
RefSeq (mRNA) NM_004041 NM_177231
RefSeq (protein) NP_004032 NP_796205
Location (UCSC) Chr 11:
74.98 – 75.06 Mb
Chr 7:
99.54 – 99.61 Mb
PubMed search [1] [2]

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

Function[edit]

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.[citation needed]

Interactions[edit]

Arrestin beta 1 has been shown to interact with

References[edit]

  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. ^ a b "Entrez Gene: ARRB1 arrestin, beta 1". 
  3. ^ 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". 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[edit]

  • 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. doi:10.1038/nature13430. PMID 25043026.  edit