Arrestin beta 1
Human protein and coding gene
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 behavior 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
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)