Arrestin beta 1

ARRB1
Uygun yapılar
PDB	Ortolog araması: PDBe RCSB
PDB kimlik kodlarının listesi
	2IV8
Tanımlayıcılar
Başka adlar	ARRB1
Dış kimlikler	OMIM: 107940 MGI: 99473 HomoloGene: 2981 GeneCards: ARRB1
Gen yerleşimi (İnsan)
Krom.	11. Kromozom (insan)
Bitiş	75,351,705 bç
RNA ekspresyonu deseni
	Daha çok ekspresyon verisi başvurusu
Gen ontolojisi
Moleküler işlevi	• GO:0005097, GO:0005099, GO:0005100 GTPase activator activity; • histone acetyltransferase activity; • GO:0048551 enzyme inhibitor activity; • insulin-like growth factor receptor binding; • transcription factor binding; • mitogen-activated protein kinase kinase binding; • clathrin adaptor activity; • protein phosphorylated amino acid binding; • cysteine-type endopeptidase inhibitor activity involved in apoptotic process; • GO:0001948, GO:0016582 protein bağlanması; • AP-2 adaptor complex binding; • alpha-1B adrenergic receptor binding; • V2 vasopressin receptor binding; • phosphoprotein binding; • angiotensin receptor binding; • ubiquitin protein ligase binding; • arrestin family protein binding; • signaling receptor binding; • enzyme binding; • estrogen receptor binding; • alpha-1A adrenergic receptor binding; • follicle-stimulating hormone receptor binding; • transmembrane transporter binding; • clathrin binding; • G protein-coupled receptor binding;
Hücresel bileşeni	• sitoplazma; • Sitozol; • postsynaptic membrane; • membrane; • hücre çekirdeği; • cell projection; • Dendritik dal; • heterotrimeric G-protein complex; • Kromatin; • Hücre zarı; • intracellular anatomical structure; • Nükleoplazma; • clathrin-coated pit; • Yalancı ayak; • GO:0097483, GO:0097481 postsynaptic density; • Golgi membrane; • lysosomal membrane; • basolateral plasma membrane; • cytoplasmic vesicle membrane; • GO:0016023 cytoplasmic vesicle; • nuclear body; • Endozom;
Biyolojik süreci	• positive regulation of Rho protein signal transduction; • regulation of G protein-coupled receptor signaling pathway; • positive regulation of receptor internalization; • transcription by RNA polymerase II; • stress fiber assembly; • follicle-stimulating hormone signaling pathway; • platelet activation; • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; • GO:0034259 negative regulation of GTPase activity; • positive regulation of ERK1 and ERK2 cascade; • positive regulation of insulin secretion involved in cellular response to glucose stimulus; • proteasome-mediated ubiquitin-dependent protein catabolic process; • phototransduction; • GO:0009373 regulation of transcription, DNA-templated; • transcription, DNA-templated; • positive regulation of peptidyl-serine phosphorylation; • negative regulation of interleukin-8 production; • protein ubiquitination; • protein transport; • GO:0033128 negative regulation of protein phosphorylation; • positive regulation of smooth muscle cell apoptotic process; • positive regulation of histone H4 acetylation; • positive regulation of protein binding; • negative regulation of NF-kappaB transcription factor activity; • positive regulation of protein ubiquitination; • G protein-coupled receptor internalization; • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; • Endositoz; • negative regulation of interleukin-6 production; • positive regulation of histone acetylation; • negative regulation of protein ubiquitination; • negative regulation of ERK1 and ERK2 cascade; • negative regulation of signal transduction; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • GO:0072468 Sinyal transdüksiyonu; • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity; • GO:0097285 apoptoz; • membrane organization; • regulation of apoptotic process; • ubiquitin-dependent protein catabolic process; • negative regulation of Notch signaling pathway; • G protein-coupled receptor signaling pathway; • positive regulation of protein phosphorylation; • positive regulation of cell population proliferation; • negative regulation of apoptotic process; • GO:1904089 negative regulation of neuron apoptotic process; • histone acetylation;
	Kaynaklar:Amigo / QuickGO
Ortologlar
	408
	109689
	ENSG00000137486
	ENSMUSG00000018909
	P49407
	Q8BWG8
	NM_004041; NM_020251
	NM_177231; NM_178220
	NP_004032; NP_064647
	NP_796205; NP_835738
	Vikiveri
İnsan'ı Gör/Düzenle	Fare'yi Gör/Düzenle

Arrestin beta 1 (ARRB1 olarak da bilinir), insanlarda ARRB1 geni tarafından kodlanan bir proteindir.^[4]^[5]

İşlev

Arrestin/beta arrestin proteini ailesinin üyelerinin, G proteini kenetli reseptörlerin agonist aracılı duyarsızlaşmasına katıldıkları ve hormonlar, nörotransmitterler veya duyusal sinyaller gibi uyaranlara hücresel yanıtların özgül olarak azaltılmasına neden oldukları düşünülmektedir. Arrestin beta 1, sitozolik bir proteindir ve beta adrenerjik reseptör kinaz (BARK) aracılı beta-adrenerjik reseptörlerin duyarsızlaştırılmasında bir kofaktör görevi görür. Merkezi sinir sisteminin yanı sıra, periferik kan lökositlerinde yüksek düzeylerde dışa vurulur ve bu nedenle BARK/beta arrestin sisteminin reseptör aracılı bağışıklık işlevlerinin düzenlenmesinde önemli bir rol oynadığına inanılmaktadır. Arrestin beta 1'in farklı izoformlarını kodlayan alternatif olarak uçbirleştirilmiş transkriptler tanımlanmıştır, ancak bunların kesin işlevleri bilinmemektedir.^[5] Beta arrestin ayrıca GPCR yollarında yapı iskelesi proteini olarak da rol oynayabilir.^{[kaynak belirtilmeli]}

Etkileşimler

Aşağıda arrestin beta 1 ile etkileşime girenler gösterilmiştir:

Arf6,^[6]
PTHLH,^[7]
DVL2,^[8]
Mdm2,^[9]^[10]
OPRD1,^[11]
PSCD2 ve
RALGDS.^[12]

Kaynakça

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000137486 - Ensembl, May 2017
^ "İnsan PubMed Başvurusu:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Fare PubMed Başvurusu:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "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). Mayıs 1993. ss. 9753-61. 3 Ocak 2005 tarihinde kaynağından arşivlendi. Erişim tarihi: 4 Mart 2020.
^ ^a ^b "Entrez Gene: ARRB1 arrestin, beta 1". 5 Aralık 2010 tarihinde kaynağından arşivlendi.
^ "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45). Kasım 2001. ss. 42509-13.
^ "The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B". FEBS Lett. 527 (1-3). Eylül 2002. ss. 71-5.
^ "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proc. Natl. Acad. Sci. U.S.A. 98 (26). Aralık 2001. ss. 14889-94.
^ "Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus". J. Biol. Chem. 278 (13). Mart 2003. ss. 11648-53.
^ "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". J. Biol. Chem. 283 (32). Ağustos 2008. ss. 22166-76.
^ "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". J. Neurochem. 76 (6). Mart 2001. ss. 1887-94.
^ "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nat. Cell Biol. 4 (8). Ağustos 2002. ss. 547-55.

Konuyla ilgili yayınlar

Lefkowitz RJ (1998). "G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization". J. Biol. Chem. 273 (30). ss. 18677-80. doi:10.1074/jbc.273.30.18677. PMID 9668034.
Lohse MJ, Benovic JL, Codina J (1990). "beta-Arrestin: a protein that regulates beta-adrenergic receptor function". Science. 248 (4962). ss. 1547-50. doi:10.1126/science.2163110. PMID 2163110.
Calabrese G, Sallese M, Stornaiuolo A (1995). "Assignment of the beta-arrestin 1 gene (ARRB1) to human chromosome 11q13". Genomics. 24 (1). ss. 169-71. doi:10.1006/geno.1994.1594. PMID 7896272.
Parruti G, Peracchia F, Sallese M (1993). "Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing". J. Biol. Chem. 268 (13). ss. 9753-61. PMID 8486659.
Iacovelli L, Franchetti R, Masini M, De Blasi A (1997). "GRK2 and beta-arrestin 1 as negative regulators of thyrotropin receptor-stimulated response". Mol. Endocrinol. 10 (9). ss. 1138-46. doi:10.1210/me.10.9.1138. PMID 8885248.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9). ss. 791-806. doi:10.1101/gr.6.9.791. PMID 8889548.
Goodman OB, Krupnick JG, Gurevich VV (1997). "Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain". J. Biol. Chem. 272 (23). ss. 15017-22. doi:10.1074/jbc.272.23.15017. PMID 9169477.
Lin FT, Krueger KM, Kendall HE (1998). "Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1". J. Biol. Chem. 272 (49). ss. 31051-7. doi:10.1074/jbc.272.49.31051. PMID 9388255.
Aragay AM, Mellado M, Frade JM (1998). "Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2". Proc. Natl. Acad. Sci. U.S.A. 95 (6). ss. 2985-90. doi:10.1073/pnas.95.6.2985. PMC 19681 $2. PMID 9501202.
ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker". Cell. 95 (4). ss. 563-73. doi:10.1016/S0092-8674(00)81623-2. PMC 4428171 $2. PMID 9827808.
Luttrell LM, Ferguson SS, Daaka Y (1999). "Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes". Science. 283 (5402). ss. 655-61. doi:10.1126/science.283.5402.655. PMID 9924018.
McDonald PH, Cote NL, Lin FT (1999). "Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation". J. Biol. Chem. 274 (16). ss. 10677-80. doi:10.1074/jbc.274.16.10677. PMID 10196135.
Lin FT, Miller WE, Luttrell LM, Lefkowitz RJ (1999). "Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases". J. Biol. Chem. 274 (23). ss. 15971-4. doi:10.1074/jbc.274.23.15971. PMID 10347142.
McConalogue K, Déry O, Lovett M (1999). "Substance P-induced trafficking of beta-arrestins. The role of beta-arrestins in endocytosis of the neurokinin-1 receptor". J. Biol. Chem. 274 (23). ss. 16257-68. doi:10.1074/jbc.274.23.16257. PMID 10347182.
Miller WE, Maudsley S, Ahn S (2000). "beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis". J. Biol. Chem. 275 (15). ss. 11312-9. doi:10.1074/jbc.275.15.11312. PMID 10753943.
Laporte SA, Oakley RH, Holt JA (2000). "The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits". J. Biol. Chem. 275 (30). ss. 23120-6. doi:10.1074/jbc.M002581200. PMID 10770944.
Bennett TA, Maestas DC, Prossnitz ER (2000). "Arrestin binding to the G protein-coupled N-formyl peptide receptor is regulated by the conserved "DRY" sequence". J. Biol. Chem. 275 (32). ss. 24590-4. doi:10.1074/jbc.C000314200. PMID 10823817.
Shiina T, Kawasaki A, Nagao T, Kurose H (2000). "Interaction with beta-arrestin determines the difference in internalization behavor between beta1- and beta2-adrenergic receptors". J. Biol. Chem. 275 (37). ss. 29082-90. doi:10.1074/jbc.M909757199. PMID 10862778.
Barlic J, Andrews JD, Kelvin AA (2001). "Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI". Nat. Immunol. 1 (3). ss. 227-33. doi:10.1038/79767. PMID 10973280.
Shukla, A. K.; Westfield, G. H.; Xiao, K; Reis, R. I.; Huang, L. Y.; Tripathi-Shukla, P; Qian, J; Li, S; Blanc, A; Oleskie, A. N.; Dosey, A. M.; Su, M; Liang, C. R.; Gu, L. L.; Shan, J. M.; Chen, X; Hanna, R; Choi, M; Yao, X. J.; Klink, B. U.; Kahsai, A. W.; Sidhu, S. S.; Koide, S; Penczek, P. A.; Kossiakoff, A. A.; Woods Jr, V. L.; Kobilka, B. K.; Skiniotis, G; Lefkowitz, R. J. (2014). "Visualization of arrestin recruitment by a G-protein-coupled receptor". Nature. Cilt 512. ss. 218-22. doi:10.1038/nature13430. PMC 4134437 $2. PMID 25043026.

Dış bağlantılar

İnsan ARRB130 Aralık 2019 tarihinde Wayback Machine sitesinde arşivlendi. genom yerleşimi ve ARRB1^{[ölü/kırık bağlantı]} geni ayrıntıları sayfası UCSC Genom Tarayıcısında.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000137486 - Ensembl, May 2017

[2] "İnsan PubMed Başvurusu:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Fare PubMed Başvurusu:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8486659-4] "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). Mayıs 1993. ss. 9753-61. 3 Ocak 2005 tarihinde kaynağından arşivlendi. Erişim tarihi: 4 Mart 2020.

[entrez-5] "Entrez Gene: ARRB1 arrestin, beta 1". 5 Aralık 2010 tarihinde kaynağından arşivlendi.

[pmid11533043-6] "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". J. Biol. Chem. 276 (45). Kasım 2001. ss. 42509-13.

[pmid12220636-7] "The COOH-terminus of parathyroid hormone-related protein (PTHrP) interacts with beta-arrestin 1B". FEBS Lett. 527 (1-3). Eylül 2002. ss. 71-5.

[pmid11742073-8] "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proc. Natl. Acad. Sci. U.S.A. 98 (26). Aralık 2001. ss. 14889-94.

[pmid12538596-9] "Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus". J. Biol. Chem. 278 (13). Mart 2003. ss. 11648-53.

[pmid18544533-10] "Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor". J. Biol. Chem. 283 (32). Ağustos 2008. ss. 22166-76.

[pmid11259507-11] "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". J. Neurochem. 76 (6). Mart 2001. ss. 1887-94.

[pmid12105416-12] "Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization". Nat. Cell Biol. 4 (8). Ağustos 2002. ss. 547-55.

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