Arrestin beta 2
(Redirected from
Β-arrestin 2
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| Location (UCSC) | Chr 17: 4.71 – 4.72 Mb | Chr 11: 70.32 – 70.33 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
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Beta-arrestin-2, also known as arrestin beta-2, is an intracellular protein that in humans is encoded by the ARRB2 gene.
Members of
alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.[13]
The protein may interact with the agonist DOI in 5-HT2A receptor signaling.[14][15]
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
- ^ a b c GRCh38: Ensembl release 89: ENSG00000141480 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060216 – 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.
- PMID 18622177.
- PMID 19399231.
- PMID 17947509.
- PMID 17215450.
- PMID 18037927.
- PMID 18268361.
- PMID 19103204.
- PMID 19442183.
- ^ "ARRB2 arrestin beta 2 [ Homo sapiens (human) ]". National Center for Biotechnology Information.
- PMID 18195357.
- PMID 18195368.
- PMID 10097102.
- PMID 12070169.
- PMID 11533043.
- PMID 12488444.
- PMID 12538596.
- PMID 18544533.
- 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): 18677–80. PMID 9668034.
- Attramadal H, Arriza JL, Aoki C, Dawson TM, Codina J, Kwatra MM, Snyder SH, Caron MG, Lefkowitz RJ (September 1992). "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family". The Journal of Biological Chemistry. 267 (25): 17882–90. PMID 1517224.
- Rapoport B, Kaufman KD, Chazenbalk GD (April 1992). "Cloning of a member of the arrestin family from a human thyroid cDNA library". Molecular and Cellular Endocrinology. 84 (3): R39-43. S2CID 1964362.
- Calabrese G, Sallese M, Stornaiuolo A, Stuppia L, Palka G, De Blasi A (September 1994). "Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes". Genomics. 23 (1): 286–8. PMID 7695743.
- 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.
- Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J (February 1997). "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. S2CID 21074692.
- Barak LS, Ferguson SS, Zhang J, Caron MG (October 1997). "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation". The Journal of Biological Chemistry. 272 (44): 27497–500. PMID 9346876.
- Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS (March 1999). "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. PMID 10097102.
- Cheng ZJ, Zhao J, Sun Y, Hu W, Wu YL, Cen B, Wu GX, Pei G (January 2000). "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. PMID 10644702.
- Lin F, Wang Hy, Malbon CC (June 2000). "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". The Journal of Biological Chemistry. 275 (25): 19025–34. PMID 10858453.
- McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ (November 2000). "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science. 290 (5496): 1574–7. PMID 11090355.
- Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ (February 2001). "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. PMID 11226259.
- 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". Journal of Neurochemistry. 76 (6): 1887–94. S2CID 83485138.
- Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG (June 2001). "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. PMID 11279203.
- Miller WE, McDonald PH, Cai SF, Field ME, Davis RJ, Lefkowitz RJ (July 2001). "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. PMID 11356842.
- 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): 42509–13. PMID 11533043.
- Hilairet S, Bélanger C, Bertrand J, Laperrière A, Foord SM, Bouvier M (November 2001). "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. PMID 11535606.
- Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ (November 2001). "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin". Science. 294 (5545): 1307–13. S2CID 23486946.
- Chen Z, Dupré DJ, Le Gouill C, Rola-Pleszczynski M, Stanková J (March 2002). "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. 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.