From Wikipedia, the free encyclopedia
ARRB2
Identifiers
Aliases ARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
External IDs OMIM: 107941; MGI: 99474; HomoloGene: 3183; GeneCards: ARRB2; OMA: ARRB2 - orthologs
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 Mb Chr 11: 70.32 – 70.33 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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

Arrestin beta 2 has been shown to interact with

References

  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

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


From Wikipedia, the free encyclopedia
ARRB2
Identifiers
Aliases ARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
External IDs OMIM: 107941; MGI: 99474; HomoloGene: 3183; GeneCards: ARRB2; OMA: ARRB2 - orthologs
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 Mb Chr 11: 70.32 – 70.33 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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

Arrestin beta 2 has been shown to interact with

References

  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

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



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