Biology:Arrestin beta 2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Beta-arrestin-2, also known as arrestin beta-2, is an intracellular protein that in humans is encoded by the ARRB2 gene.
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,[1][2][3] as well as having signalling roles in their own right.[4][5][6][7][8] Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.[9]
The protein may interact with the agonist DOI in 5-HT2A receptor signaling.[10][11]
Arrestin beta 2 is crucial for the development of tolerance to morphine and other opioids.
Interactions
Arrestin beta 2 has been shown to interact with
References
- ↑ "Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice". Behavioural Pharmacology 19 (4): 298–307. July 2008. doi:10.1097/FBP.0b013e328308f1e6. PMID 18622177.
- ↑ "Improvement of morphine-mediated analgesia by inhibition of β-arrestin2 expression in mice periaqueductal gray matter". International Journal of Molecular Sciences 10 (3): 954–63. March 2009. doi:10.3390/ijms10030954. PMID 19399231.
- ↑ "Beta-arrestin-dependent mu-opioid receptor-activated extracellular signal-regulated kinases (ERKs) Translocate to Nucleus in Contrast to G protein-dependent ERK activation". Molecular Pharmacology 73 (1): 178–90. January 2008. doi:10.1124/mol.107.039842. PMID 17947509.
- ↑ "Beta-arrestin signaling and regulation of transcription". Journal of Cell Science 120 (Pt 2): 213–8. January 2007. doi:10.1242/jcs.03338. PMID 17215450.
- ↑ "Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction". British Journal of Pharmacology 153 Suppl 1 (S1): S298-309. March 2008. doi:10.1038/sj.bjp.0707508. PMID 18037927.
- ↑ "Beta-arrestins: multifunctional cellular mediators". Physiology 23: 17–22. February 2008. doi:10.1152/physiol.00042.2007. PMID 18268361.
- ↑ "Physiologic and cardiac roles of beta-arrestins". Journal of Molecular and Cellular Cardiology 46 (3): 300–8. March 2009. doi:10.1016/j.yjmcc.2008.11.015. PMID 19103204.
- ↑ "Antidepressants, beta-arrestins and GRKs: from regulation of signal desensitization to intracellular multifunctional adaptor functions". Current Pharmaceutical Design 15 (14): 1699–708. 2009. doi:10.2174/138161209788168038. PMID 19442183.
- ↑ "ARRB2 arrestin beta 2 [ Homo sapiens (human) "]. National Center for Biotechnology Information. https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=409.
- ↑ "Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo". Proceedings of the National Academy of Sciences of the United States of America 105 (3): 1079–84. January 2008. doi:10.1073/pnas.0708862105. PMID 18195357.
- ↑ "Arresting serotonin". Proceedings of the National Academy of Sciences of the United States of America 105 (3): 831–2. January 2008. doi:10.1073/pnas.0711335105. PMID 18195368. Bibcode: 2008PNAS..105..831A.
- ↑ "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proceedings of the National Academy of Sciences of the United States of America 96 (7): 3712–7. March 1999. doi:10.1073/pnas.96.7.3712. PMID 10097102. Bibcode: 1999PNAS...96.3712L.
- ↑ "Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking". The Journal of Biological Chemistry 277 (34): 30760–8. August 2002. doi:10.1074/jbc.M204528200. PMID 12070169.
- ↑ "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry 276 (45): 42509–13. November 2001. doi:10.1074/jbc.M108399200. PMID 11533043.
- ↑ "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2". The Journal of Biological Chemistry 278 (8): 6363–70. February 2003. doi:10.1074/jbc.M210350200. PMID 12488444.
- ↑ "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): 11648–53. March 2003. doi:10.1074/jbc.M208109200. PMID 12538596.
- ↑ "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". The Journal of Biological Chemistry 283 (32): 22166–76. August 2008. doi:10.1074/jbc.M709668200. PMID 18544533.
- ↑ "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nature Cell Biology 4 (8): 547–55. August 2002. doi:10.1038/ncb821. PMID 12105416.
Further reading
- "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): 18677–80. July 1998. doi:10.1074/jbc.273.30.18677. PMID 9668034.
- "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family". The Journal of Biological Chemistry 267 (25): 17882–90. September 1992. doi:10.1016/S0021-9258(19)37125-X. PMID 1517224.
- "Cloning of a member of the arrestin family from a human thyroid cDNA library". Molecular and Cellular Endocrinology 84 (3): R39-43. April 1992. doi:10.1016/0303-7207(92)90038-8. PMID 1587386.
- "Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes". Genomics 23 (1): 286–8. September 1994. doi:10.1006/geno.1994.1497. PMID 7695743.
- "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. May 1993. doi:10.1016/S0021-9258(18)98412-7. PMID 8486659.
- "Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor". FEBS Letters 402 (2–3): 203–8. February 1997. doi:10.1016/S0014-5793(96)01531-1. PMID 9037196.
- "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation". The Journal of Biological Chemistry 272 (44): 27497–500. October 1997. doi:10.1074/jbc.272.44.27497. PMID 9346876.
- "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis". Proceedings of the National Academy of Sciences of the United States of America 96 (7): 3712–7. March 1999. doi:10.1073/pnas.96.7.3712. PMID 10097102. Bibcode: 1999PNAS...96.3712L.
- "beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4". The Journal of Biological Chemistry 275 (4): 2479–85. January 2000. doi:10.1074/jbc.275.4.2479. PMID 10644702.
- "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". The Journal of Biological Chemistry 275 (25): 19025–34. June 2000. doi:10.1074/jbc.275.25.19025. PMID 10858453.
- "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science 290 (5496): 1574–7. November 2000. doi:10.1126/science.290.5496.1574. PMID 11090355. Bibcode: 2000Sci...290.1574M.
- "Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds". Proceedings of the National Academy of Sciences of the United States of America 98 (5): 2449–54. February 2001. doi:10.1073/pnas.041604898. PMID 11226259. Bibcode: 2001PNAS...98.2449L.
- "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". Journal of Neurochemistry 76 (6): 1887–94. March 2001. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507.
- "Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*". The Journal of Biological Chemistry 276 (22): 19452–60. June 2001. doi:10.1074/jbc.M101450200. PMID 11279203.
- "Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3". The Journal of Biological Chemistry 276 (30): 27770–7. July 2001. doi:10.1074/jbc.M102264200. PMID 11356842.
- "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry 276 (45): 42509–13. November 2001. doi:10.1074/jbc.M108399200. PMID 11533043.
- "Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin". The Journal of Biological Chemistry 276 (45): 42182–90. November 2001. doi:10.1074/jbc.M107323200. PMID 11535606.
- "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin". Science 294 (5545): 1307–13. November 2001. doi:10.1126/science.1063866. PMID 11588219. Bibcode: 2001Sci...294.1307S.
- "Agonist-induced internalization of the platelet-activating factor receptor is dependent on arrestins but independent of G-protein activation. Role of the C terminus and the (D/N)PXXY motif". The Journal of Biological Chemistry 277 (9): 7356–62. March 2002. doi:10.1074/jbc.M110058200. PMID 11729201.
External links
- Human ARRB2 genome location and ARRB2 gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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