Arrestin beta 2

From Wikipedia the free encyclopedia

ARRB2
Identifiers
AliasesARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
External IDsOMIM: 107941 MGI: 99474 HomoloGene: 3183 GeneCards: ARRB2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001271358
NM_001271359
NM_001271360
NM_145429

RefSeq (protein)

NP_001258287
NP_001258288
NP_001258289
NP_663404

Location (UCSC)Chr 17: 4.71 – 4.72 MbChr 11: 70.32 – 70.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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,[5][6][7] as well as having signalling roles in their own right.[8][9][10][11][12] 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.[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[edit]

Arrestin beta 2 has been shown to interact with

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000141480Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000060216Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ Li Y, Liu X, Liu C, Kang J, Yang J, Pei G, Wu C (March 2009). "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. doi:10.3390/ijms10030954. PMC 2672012. PMID 19399231.
  7. ^ 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.
  8. ^ 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.
  9. ^ Defea K (March 2008). "Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction". British Journal of Pharmacology. 153 Suppl 1 (S1): S298-309. doi:10.1038/sj.bjp.0707508. PMC 2268080. PMID 18037927.
  10. ^ Barki-Harrington L, Rockman HA (February 2008). "Beta-arrestins: multifunctional cellular mediators". Physiology. 23: 17–22. doi:10.1152/physiol.00042.2007. PMID 18268361.
  11. ^ 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.
  12. ^ 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.
  13. ^ "ARRB2 arrestin beta 2 [ Homo sapiens (human) ]". National Center for Biotechnology Information.
  14. ^ Schmid CL, Raehal KM, Bohn LM (January 2008). "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. doi:10.1073/pnas.0708862105. PMC 2242710. PMID 18195357.
  15. ^ Abbas A, Roth BL (January 2008). "Arresting serotonin". Proceedings of the National Academy of Sciences of the United States of America. 105 (3): 831–2. Bibcode:2008PNAS..105..831A. doi:10.1073/pnas.0711335105. PMC 2242676. PMID 18195368.
  16. ^ 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. Bibcode:1999PNAS...96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
  17. ^ Kim YM, Benovic JL (August 2002). "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. doi:10.1074/jbc.M204528200. PMID 12070169.
  18. ^ 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. doi:10.1074/jbc.M108399200. PMID 11533043.
  19. ^ 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". The Journal of Biological Chemistry. 278 (8): 6363–70. doi:10.1074/jbc.M210350200. PMID 12488444.
  20. ^ 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): 11648–53. doi:10.1074/jbc.M208109200. PMID 12538596.
  21. ^ 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): 22166–76. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533.
  22. ^ 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". Nature Cell Biology. 4 (8): 547–55. doi:10.1038/ncb821. PMID 12105416. S2CID 20784208.

Further reading[edit]

External links[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.