Arrestin beta 2

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

ARRB2
Tanımlayıcılar
	ARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
Xarici ID-lər	107941 99474 3183 ARRB2
Genin yeri (İnsan) Xromosom Lokus 17p13.2 Başlanğıc 4,710,596 Son 4,721,499
Genin yeri (Siçan) Xromosom Xromosom 11 (siçan) Lokus 11 B3|11 42.99 cM Başlanğıc 70,323,461 Son 70,331,654
İfadə məlumatı üçün daha çox istinad
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
Species	Human	Mouse
	409	216869
	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 Mb	Chr 11: 70.32 – 70.33 Mb
axtarışı
Wikidata
İnsanı göstər/redaktə et Siçanı göstər/redaktə 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. Arrestin beta 2 zülalı həmçinin müstəqil siqnal roluna malikdir.

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 DNTqalxanabənzər 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 siqnalında agonist DOI ilə qarşılıqlı əlaqədə ola bilər.

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

Qarşılıqlı əlaqələri

Arrestin beta 2 ilə qarşılıqlı əlaqədə olanlar:

• AP2B1,
• PSCD2,
• Mdm2, və
• RALGDS.

İstinadlar

1. GRCh38: Ensembl release 89: ENSG00000141480 - , May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000060216 - , May 2017
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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.
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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.
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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.
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• 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.
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• 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.
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• 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.
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• 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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