Arrestin beta 2

ARRB2
Tanımlayıcılar
Digər adları	ARRB2, ARB2, ARR2, BARR2, Arrestin beta 2
Xarici ID-lər	OMIM: 107941 MGI: 99474 HomoloGene: 3183 GeneCards: ARRB2
Genin yeri (İnsan) Xromosom Xromosom 17 (insan) Lokus 17p13.2 Başlanğıc 4,710,596 cb Son 4,721,499 bp
Genin yeri (Siçan) Xromosom Xromosom 11 (siçan) Lokus 11 B3|11 42.99 cM Başlanğıc 70,323,461 bp Son 70,331,654 bp
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
Species	Human	Mouse
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 Mb	Chr 11: 70.32 – 70.33 Mb
PubMed axtarışı
Wikidata
İnsanı göstər/redaktə et Siçanı göstər/redaktə et

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

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 DNT 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 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.

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.