| edit |
| Arestin beta 2 | |||||||||
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| Identifikatori | |||||||||
| Simboli | ARRB2; ARB2; ARR2; DKFZp686L0365 | ||||||||
| Vanjski ID | OMIM: 107941 MGI: 99474 HomoloGene: 3183 GeneCards: ARRB2 Gene | ||||||||
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| Pregled RNK izražavanja | |||||||||
| 👁 Image | |||||||||
| podaci | |||||||||
| Ortolozi | |||||||||
| Vrsta | Čovek | Miš | |||||||
| Entrez | 409 | 216869 | |||||||
| Ensembl | ENSG00000141480 | ENSMUSG00000060216 | |||||||
| UniProt | P32121 | Q3UCU5 | |||||||
| RefSeq (mRNA) | NM_004313 | XM_993633 | |||||||
| RefSeq (protein) | NP_004304 | XP_998727 | |||||||
| Lokacija (UCSC) | Chr 17: 4.56 - 4.57 Mb | Chr 11: 70.25 - 70.26 Mb | |||||||
| PubMed pretraga | [1] | [2] | |||||||
Arestin beta 2 (Beta arestin 2) je intracelularni protein koji je kod čoveka kodiran ARRB2 genom.
Za članove arestin/beta-arestin proteinske familije se smatra da učestvuju u agonistom-posredovanoj desenzitizaciji G protein-spregnutih receptora i izazivaju specifično prigušenje ćelijskog odgovora na stimuluse kao što su hormoni, neurotransmiteri, ili senzorne signale,[1][2][3] kao i da imaju zasebne signalne uloge.[4][5][6][7][8] Za arestin beta 2, poput arestina beta 1, je pokazano da inhibira funkciju beta-adrenergičkog receptora in vitro. On je izražen u visokim nivoima u centralnom nervnom sistemu i učestvuje u regulaciji sinaptičkih receptora. Pored mozga, cDNK za arestin beta 2 je bila izolovana iz tiroidne žlezde, i stoga on možda učestvuje u hormon-specifičnoj desenzitizaciji TSH receptora. Više alternativno splajsovanih transkriptnih varijanti ovog gena je nađeno.[9]
Ovaj protein može da interaguje sa agonistom DOI u signalizaciji 5-HT2A receptora.[10][11]
Za arestin beta 2 je pokazano da interaguje sa
- ↑ Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK (July 2008). „Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice”. Behavioural Pharmacology 19 (4): 298–307. DOI:10.1097/FBP.0b013e328308f1e6. PMC 2751575. PMID 18622177.
- ↑ Li Y, Liu X, Liu C, Kang J, Yang J, Pei G, Wu C (March 2009). „Improvement of Morphine-Mediated Analgesia by Inhibition of beta-Arrestin 2 Expression in Mice Periaqueductal Gray Matter”. International Journal of Molecular Sciences 10 (3): 954–63. DOI:10.3390/ijms10030954. PMC 2672012. PMID 19399231.
- ↑ Zheng H, Loh HH, Law PY (January 2008). „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. DOI:10.1124/mol.107.039842. PMC 2253657. PMID 17947509.
- ↑ Ma L, Pei G (January 2007). „Beta-arrestin signaling and regulation of transcription”. Journal of Cell Science 120 (Pt 2): 213–8. DOI:10.1242/jcs.03338. PMID 17215450.
- ↑ Defea K (March 2008). „Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction”. British Journal of Pharmacology 153 Suppl 1: S298–309. DOI:10.1038/sj.bjp.0707508. PMC 2268080. PMID 18037927.
- ↑ Barki-Harrington L, Rockman HA (February 2008). „Beta-arrestins: multifunctional cellular mediators”. Physiology (Bethesda, Md.) 23: 17–22. DOI:10.1152/physiol.00042.2007. PMID 18268361.
- ↑ Patel PA, Tilley DG, Rockman HA (March 2009). „Physiologic and cardiac roles of beta-arrestins”. Journal of Molecular and Cellular Cardiology 46 (3): 300–8. DOI:10.1016/j.yjmcc.2008.11.015. PMID 19103204.
- ↑ Golan M, Schreiber G, Avissar S (2009). „Antidepressants, beta-arrestins and GRKs: from regulation of signal desensitization to intracellular multifunctional adaptor functions”. Current Pharmaceutical Design 15 (14): 1699–708. DOI:10.2174/138161209788168038. PMID 19442183.
- ↑ „Entrez Gene: ARRB2 arrestin, beta 2”.
- ↑ Schmid CL, Raehal KM, Bohn LM (January 2008). „Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo”. Proc. Natl. Acad. Sci. U.S.A. 105 (3): 1079–84. DOI:10.1073/pnas.0708862105. PMC 2242710. PMID 18195357.
- ↑ Abbas A, Roth BL (January 2008). „Arresting serotonin”. Proc. Natl. Acad. Sci. U.S.A. 105 (3): 831–2. DOI:10.1073/pnas.0711335105. PMC 2242676. PMID 18195368.
- ↑ 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”. Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. DOI:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
- ↑ Kim YM, Benovic JL (August 2002). „Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking”. J. Biol. Chem. 277 (34): 30760–8. DOI:10.1074/jbc.M204528200. PMID 12070169.
- ↑ 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.
- ↑ Wang P, Gao H, Ni Y, Wang B, Wu Y, Ji L, Qin L, Ma L, Pei G (February 2003). „Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2”. J. Biol. Chem. 278 (8): 6363–70. DOI:10.1074/jbc.M210350200. PMID 12488444.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- 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.
- Attramadal H, Arriza JL, Aoki C, et al. (1992). „Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family.”. J. Biol. Chem. 267 (25): 17882–90. PMID 1517224.
- Rapoport B, Kaufman KD, Chazenbalk GD (1992). „Cloning of a member of the arrestin family from a human thyroid cDNA library.”. Mol. Cell. Endocrinol. 84 (3): R39–43. DOI:10.1016/0303-7207(92)90038-8. PMID 1587386.
- Calabrese G, Sallese M, Stornaiuolo A, et al. (1995). „Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes.”. Genomics 23 (1): 286–8. DOI:10.1006/geno.1994.1497. PMID 7695743.
- 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.
- Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J (1997). „Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor.”. FEBS Lett. 402 (2-3): 203–8. DOI:10.1016/S0014-5793(96)01531-1. PMID 9037196.
- Barak LS, Ferguson SS, Zhang J, Caron MG (1997). „A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation.”. J. Biol. Chem. 272 (44): 27497–500. DOI:10.1074/jbc.272.44.27497. PMID 9346876.
- Laporte SA, Oakley RH, Zhang J, et al. (1999). „The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis.”. Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. DOI:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
- Cheng ZJ, Zhao J, Sun Y, et al. (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.”. J. Biol. Chem. 275 (4): 2479–85. DOI:10.1074/jbc.275.4.2479. PMID 10644702.
- Lin F, Wang H, Malbon CC (2000). „Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization.”. J. Biol. Chem. 275 (25): 19025–34. DOI:10.1074/jbc.275.25.19025. PMID 10858453.
- McDonald PH, Chow CW, Miller WE, et al. (2000). „Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3.”. Science 290 (5496): 1574–7. DOI:10.1126/science.290.5496.1574. PMID 11090355.
- Luttrell LM, Roudabush FL, Choy EW, et al. (2001). „Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds.”. Proc. Natl. Acad. Sci. U.S.A. 98 (5): 2449–54. DOI:10.1073/pnas.041604898. PMC 30158. PMID 11226259.
- Cen B, Yu Q, Guo J, et al. (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.
- Oakley RH, Laporte SA, Holt JA, et al. (2001). „Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*.”. J. Biol. Chem. 276 (22): 19452–60. DOI:10.1074/jbc.M101450200. PMID 11279203.
- Miller WE, McDonald PH, Cai SF, et al. (2001). „Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3.”. J. Biol. Chem. 276 (30): 27770–7. DOI:10.1074/jbc.M102264200. PMID 11356842.
- Claing A, Chen W, Miller WE, et al. (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.
- Hilairet S, Bélanger C, Bertrand J, et al. (2001). „Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin.”. J. Biol. Chem. 276 (45): 42182–90. DOI:10.1074/jbc.M107323200. PMID 11535606.
- Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ (2001). „Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin.”. Science 294 (5545): 1307–13. DOI:10.1126/science.1063866. PMID 11588219.
- Chen Z, Dupré DJ, Le Gouill C, et al. (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.”. J. Biol. Chem. 277 (9): 7356–62. DOI:10.1074/jbc.M110058200. PMID 11729201.