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Arrestin beta 2

  • Məqalə
  • Müzakirə

Arrestin beta 2, həmçinin arrestin beta-2 olaraq da bilinir — insanlarda ARRB2 geni ilə kodlanan hüceyrədaxili zülal.

ARRB2
Tanımlayıcılar
Digər adlarıARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
Xarici ID-lərOMIM: 107941 MGI: 99474 HomoloGene: 3183 GeneCards: ARRB2
Genin yeri (İnsan)
Xromosom 17 (insan)
XromosomXromosom 17 (insan)[1]
Xromosom 17 (insan)
Genomic location for ARRB2
Genomic location for ARRB2
Lokus17p13.2Başlanğıc4,710,596 cb[1]
Son4,721,499 bp[1]
Genin yeri (Siçan)
Xromosom 11 (siçan)
XromosomXromosom 11 (siçan)[2]
Xromosom 11 (siçan)
Genomic location for ARRB2
Genomic location for ARRB2
Lokus11 B3|11 42.99 cMBaşlanğıc70,323,461 bp[2]
Son70,331,654 bp[2]
RNT ifadəsi
İfadə məlumatı üçün daha çox istinad
Gen ontologiyası
Molekulyar funksiya• alpha-1B adrenergic receptor binding
• 14-3-3 protein binding
• protein kinase B binding
• GO:0001948, GO:0016582 protein binding
• enzyme binding
• angiotensin receptor binding
• GO:0032947 molecular adaptor activity
• signaling receptor binding
• G protein-coupled receptor binding
• ubiquitin protein ligase binding
• identical protein binding
• arrestin family protein binding
• GO:0032403 protein-containing complex binding
• protein domain specific binding
• alpha-1A adrenergic receptor binding
• type 1 angiotensin receptor binding
• D1 dopamine receptor binding
• follicle-stimulating hormone receptor binding
• type 2A serotonin receptor binding
• platelet activating factor receptor binding
• mitogen-activated protein kinase binding
Hücrəsəl komponent• Sitoplazma
• cytosol
• postsynaptic membrane
• GO:0097483, GO:0097481 postsynaptic density
• membrane
• Membran
• endocytic vesicle
• dendritic spine
• intracellular anatomical structure
• basolateral plasma membrane
• clathrin-coated pit
• GO:0016023 cytoplasmic vesicle
• Hüceyrə nüvəsi
• intracellular membrane-bounded organelle
• endosome
Bioloji proses• proteasome-mediated ubiquitin-dependent protein catabolic process
• positive regulation of calcium ion transport
• regulation of protein phosphorylation
• negative regulation of interleukin-1 beta production
• negative regulation of protein kinase B signaling
• negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
• positive regulation of protein kinase B signaling
• positive regulation of protein phosphorylation
• endocytosis
• regulation of G protein-coupled receptor signaling pathway
• positive regulation of receptor internalization
• negative regulation of release of cytochrome c from mitochondria
• negative regulation of interleukin-6 production
• receptor internalization
• transcription by RNA polymerase II
• positive regulation of peptidyl-serine phosphorylation
• detection of temperature stimulus involved in sensory perception of pain
• follicle-stimulating hormone signaling pathway
• platelet activation
• dopamine receptor signaling pathway
• negative regulation of protein ubiquitination
• brain development
• GO:0034259 negative regulation of GTPase activity
• negative regulation of toll-like receptor signaling pathway
• protein ubiquitination
• positive regulation of DNA biosynthetic process
• positive regulation of ERK1 and ERK2 cascade
• positive regulation of peptidyl-tyrosine phosphorylation
• cell chemotaxis
• protein transport
• negative regulation of natural killer cell mediated cytotoxicity
• regulation of androgen receptor signaling pathway
• positive regulation of synaptic transmission, dopaminergic
• negative regulation of tumor necrosis factor production
• negative regulation of signal transduction
• positive regulation of protein ubiquitination
• transforming growth factor beta receptor signaling pathway
• negative regulation of NF-kappaB transcription factor activity
• negative regulation of smooth muscle cell apoptotic process
• desensitization of G protein-coupled receptor signaling pathway by arrestin
• GO:0072468 signal transduction
• adult walking behavior
• negative regulation of interleukin-12 production
• Wnt signaling pathway, planar cell polarity pathway
• GO:0033128 negative regulation of protein phosphorylation
• G protein-coupled receptor internalization
• GO:1901313 positive regulation of gene expression
• protein deubiquitination
• membrane organization
• positive regulation of cardiac muscle cell differentiation
• G protein-coupled receptor signaling pathway
• excitatory postsynaptic potential
• positive regulation of collagen biosynthetic process
• GO:1904089 negative regulation of neuron apoptotic process
• positive regulation of epithelial cell apoptotic process
Sources:Amigo / QuickGO
Ortoloqlar
SpeciesHumanMouse
Entrez

409

216869

Ensembl

ENSG00000141480

ENSMUSG00000060216

UniProt

P32121

Q91YI4

RefSeq (mRNA)
NM_001257328
NM_001257329
NM_001257330
NM_001257331
NM_004313

NM_199004
NM_001330064

NM_001271358
NM_001271359
NM_001271360
NM_145429

RefSeq (protein)
NP_001244257
NP_001244258
NP_001244259
NP_001244260
NP_001316993

NP_004304
NP_945355

NP_001258287
NP_001258288
NP_001258289
NP_663404

Yeri (UCSC)Chr 17: 4.71 – 4.72 MbChr 11: 70.32 – 70.33 Mb
PubMed axtarışı[3][4]
Wikidata
İnsanı göstər/ et Siçanı göstər/ et

Arrestin beta 2 zülal ailəsinin üzvlərinin G zülalı ilə əlaqəli reseptorların agonist vasitəçiliyi ilə desensitizasiyasında iştirak etdiyi və hormonlar, neyrotransmitterlər və ya duyğu siqnalları kimi stimullara hüceyrə reaksiyalarının spesifik şəkildə yatırılmasına səbəb olduğu düşünülür.[5][6][7] Arrestin beta 2 zülalı həmçinin müstəqil siqnal roluna malikdir.[8][9][10][11][12]

Arrestin beta 2, arrestin beta 1 kimi, beta-adrenergik reseptor funksiyasını in vitro inhibe edir. Mərkəzi sinir sistemində yüksək səviyyədə ifadə edilir və sinoptik reseptorların tənzimlənməsində rol oynaya bilər.

Beyinlə yanaşı, arrestin beta 2 üçün tamamlayıcı DNT[13] qalxanabənzər vəzindən təcrid edilmişdir və beləliklə, o, tirotropin reseptorlarının hormon-spesifik desensitizasiyasında da iştirak edə bilər. Bu gen üçün bir çox alternativ olaraq birləşdirilmiş transkript variantları tapılmışdır, lakin bəzi variantların tam aydın təbiəti müəyyən edilməmişdir.[13]

Zülal 5-HT2A reseptor[14] siqnalında agonist DOI[15] ilə qarşılıqlı əlaqədə ola bilər.[16][17]

Arrestin beta 2 morfin və digər opioidlərə[18] qarşı dözümlülüyün inkişafı üçün vacibdir.

Mündəricat

  • 1 Qarşılıqlı əlaqələri
  • 2 İstinadlar
  • 3 Ədəbiyyatı
  • 4

Qarşılıqlı əlaqələri

Arrestin beta 2 ilə qarşılıqlı əlaqədə olanlar:

  • AP2B1,[19][20]
  • PSCD2,[21]
  • Mdm2,[22][23][24] və
  • RALGDS.[25]

İstinadlar

  1. ↑ 1 2 3 GRCh38: Ensembl release 89: ENSG00000141480 - Ensembl, May 2017
  2. ↑ 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060216 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK. "Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice". Behavioural Pharmacology. 19 (4). July 2008: 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. "Improvement of morphine-mediated analgesia by inhibition of β-arrestin2 expression in mice periaqueductal gray matter". International Journal of Molecular Sciences. 10 (3). March 2009: 954–63. doi:10.3390/ijms10030954. PMC 2672012. PMID 19399231.
  7. ↑ Zheng H. "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). January 2008: 178–90. doi:10.1124/mol.107.039842. PMC 2253657. PMID 17947509.
  8. ↑ Ma L, Pei G. "Beta-arrestin signaling and regulation of transcription". Journal of Cell Science. 120 (Pt 2). January 2007: 213–8. doi:10.1242/jcs.03338. PMID 17215450.
  9. ↑ Defea K. "Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction". British Journal of Pharmacology. 153 Suppl 1 (S1). March 2008: S298–309. doi:10.1038/sj.bjp.0707508. PMC 2268080. PMID 18037927.
  10. ↑ Barki-Harrington L, Rockman HA. "Beta-arrestins: multifunctional cellular mediators". Physiology. 23. February 2008: 17–22. doi:10.1152/physiol.00042.2007. PMID 18268361.
  11. ↑ Patel PA, Tilley DG, Rockman HA. "Physiologic and cardiac roles of beta-arrestins". Journal of Molecular and Cellular Cardiology. 46 (3). March 2009: 300–8. doi:10.1016/j.yjmcc.2008.11.015. PMID 19103204.
  12. ↑ Golan M, Schreiber G, Avissar S. "Antidepressants, beta-arrestins and GRKs: from regulation of signal desensitization to intracellular multifunctional adaptor functions". Current Pharmaceutical Design. 15 (14). 2009: 1699–708. doi:10.2174/138161209788168038. PMID 19442183.
  13. ↑ "Arxivlənmiş surət". 2021-06-07 tarixində arxivləşdirilib. İstifadə tarixi: 2023-09-20.
  14. ↑ "Arxivlənmiş surət". 2023-09-03 tarixində arxivləşdirilib. İstifadə tarixi: 2023-09-21.
  15. ↑ "Arxivlənmiş surət". 2023-08-26 tarixində arxivləşdirilib. İstifadə tarixi: 2023-09-21.
  16. ↑ Schmid CL, Raehal KM, title = 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). January 2008: 1079–84. doi:10.1073/pnas.0708862105. PMC 2242710. PMID 18195357 //www.ncbi.nlm.nih.gov/pmc/articles/PMC2242710 (#bare_url_missing_title). (#missing_pipe); (#vancouver)
  17. ↑ Abbas A. "Arresting serotonin". Proceedings of the National Academy of Sciences of the United States of America. 105 (3). January 2008: 831–2. Bibcode:2008PNAS..105..831A. doi:10.1073/pnas.0711335105. PMC 2242676. PMID 18195368.
  18. ↑ "Arxivlənmiş surət". 2023-08-31 tarixində arxivləşdirilib. İstifadə tarixi: 2023-09-21.
  19. ↑ Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS. "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). March 1999: 3712–7. Bibcode:1999PNAS...96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
  20. ↑ Kim YM, Benovic JL. "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). August 2002: 30760–8. doi:10.1074/jbc.M204528200. PMID 12070169.
  21. ↑ Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ. "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry. 276 (45). November 2001: 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.
  22. ↑ Wang P, Gao H, Ni Y, Wang B, Wu Y, Ji L, Qin L, Ma L, Pei G. "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2". The Journal of Biological Chemistry. 278 (8). February 2003: 6363–70. doi:10.1074/jbc.M210350200. PMID 12488444.
  23. ↑ Wang P, Wu Y, Ge X, Ma L, Pei G. "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). March 2003: 11648–53. doi:10.1074/jbc.M208109200. PMID 12538596.
  24. ↑ Shenoy SK, Xiao K, Venkataramanan V, Snyder PM, Freedman NJ, Weissman AM. "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". The Journal of Biological Chemistry. 283 (32). August 2008: 22166–76. doi:10.1074/jbc.M709668200. PMC 2494938. PMID 18544533.
  25. ↑ Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, Feldman RD, Verdi JM, Rylett RJ, Ferguson SS. "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nature Cell Biology. 4 (8). August 2002: 547–55. doi:10.1038/ncb821. PMID 12105416.

Ədəbiyyatı

  • Lefkowitz RJ. "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). July 1998: 18677–80. doi:10.1074/jbc.273.30.18677. PMID 9668034.
  • Attramadal H, Arriza JL, Aoki C, Dawson TM, Codina J, Kwatra MM, Snyder SH, Caron MG, Lefkowitz RJ. "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family". The Journal of Biological Chemistry. 267 (25). September 1992: 17882–90. doi:10.1016/S0021-9258(19)37125-X. PMID 1517224.
  • Rapoport B, Kaufman KD, Chazenbalk GD. "Cloning of a member of the arrestin family from a human thyroid cDNA library". Molecular and Cellular Endocrinology. 84 (3). April 1992: R39–43. doi:10.1016/0303-7207(92)90038-8. PMID 1587386.
  • Calabrese G, Sallese M, Stornaiuolo A, Stuppia L, Palka G, De Blasi A. "Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes". Genomics. 23 (1). September 1994: 286–8. doi:10.1006/geno.1994.1497. PMID 7695743.
  • Parruti G, Peracchia F, Sallese M, Ambrosini G, Masini M, Rotilio D, De Blasi A. "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). May 1993: 9753–61. doi:10.1016/S0021-9258(18)98412-7. PMID 8486659.
  • Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J. "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). February 1997: 203–8. doi:10.1016/S0014-5793(96)01531-1. PMID 9037196.
  • Barak LS, Ferguson SS, Zhang J, Caron MG. "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation". The Journal of Biological Chemistry. 272 (44). October 1997: 27497–500. doi:10.1074/jbc.272.44.27497. PMID 9346876.
  • Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS. "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). March 1999: 3712–7. Bibcode:1999PNAS...96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
  • Cheng ZJ, Zhao J, Sun Y, Hu W, Wu YL, Cen B, Wu GX, Pei G. "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). January 2000: 2479–85. doi:10.1074/jbc.275.4.2479. PMID 10644702.
  • Lin F, Wang Hy, Malbon CC. "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". The Journal of Biological Chemistry. 275 (25). June 2000: 19025–34. doi:10.1074/jbc.275.25.19025. PMID 10858453.
  • McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ. "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science. 290 (5496). November 2000: 1574–7. Bibcode:2000Sci...290.1574M. doi:10.1126/science.290.5496.1574. PMID 11090355.
  • Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ. "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). February 2001: 2449–54. Bibcode:2001PNAS...98.2449L. doi:10.1073/pnas.041604898. PMC 30158. PMID 11226259.
  • Cen B, Yu Q, Guo J, Wu Y, Ling K, Cheng Z, Ma L, Pei G. "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". Journal of Neurochemistry. 76 (6). March 2001: 1887–94. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507.
  • Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG. "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). June 2001: 19452–60. doi:10.1074/jbc.M101450200. PMID 11279203.
  • Miller WE, McDonald PH, Cai SF, Field ME, Davis RJ, Lefkowitz RJ. "Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3". The Journal of Biological Chemistry. 276 (30). July 2001: 27770–7. doi:10.1074/jbc.M102264200. PMID 11356842.
  • Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ. "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry. 276 (45). November 2001: 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.
  • Hilairet S, Bélanger C, Bertrand J, Laperrière A, Foord SM, Bouvier M. "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). November 2001: 42182–90. doi:10.1074/jbc.M107323200. PMID 11535606.
  • Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ. "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin". Science. 294 (5545). November 2001: 1307–13. Bibcode:2001Sci...294.1307S. doi:10.1126/science.1063866. PMID 11588219.
  • Chen Z, Dupré DJ, Le Gouill C, Rola-Pleszczynski M, Stanková J. "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). March 2002: 7356–62. doi:10.1074/jbc.M110058200. PMID 11729201.

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