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ELISA Kit for Bovine Beta-arrestin-1

SKU : BHE13800961

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EIAAB SCIENCE INC, WUHAN

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Mfr.No.	E1993b
Alternative Names	Arrestin beta-1 ; Arrestin-2
Categories	Elisa
Function	Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phopshorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors others than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Binds phosphoinositides. Binds inositol hexakisphosphate (InsP6).
Specificity	Natural and recombinant Bovine Beta-arrestin-1
Subcellular Location	Cytoplasm Nucleus Cell membrane Membrane clathrin-coated pit Cell projection pseudopodium Cytoplasmic vesicle Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located in the nucleus. The oligomeric form is located in the cytoplasm. Translocates to the nucleus upon stimulation of OPRD1.
Entryname	ARRB1_BOVIN
Platform	PF02752
Protein Name	Beta-arrestin-1
Sequence	50: MGDKGTRVFK ; KASPNGKLTV ; YLGKRDFVDH ; IDLVEPVDGV ; VLVDPEYLKE ; 100: RRVYVTLTCA ; FRYGREDLDV ; LGLTFRKDLF ; VANVQSFPPA ; PEDKKPLTRL ; 150: QERLIKKLGE ; HAYPFTFEIP ; PNLPCSVTLQ ; PGPEDTGKAC ; GVDYEVKAFC ; 200: AENLEEKIHK ; RNSVRLVIRK ; VQYAPERPGP ; QPTAETTRQF ; LMSDKPLHLE ; 250: ASLDKEIYYH ; GEPISVNVHV ; TNNTNKTVKK ; IKISVRQYAD ; ICLFNTAQYK ; 300: CPVAMEEADD ; TVAPSSTFCK ; VYTLTPFLAN ; NREKRGLALD ; GKLKHEDTNL ; 350: ASSTLLREGA ; NREILGIIVS ; YKVKVKLVVS ; RGGLLGDLAS ; SDVAVELPFT ; 400: LMHPKPKEEP ; PHREVPEHET ; PVDTNLIELD ; TNDDDIVFED ; FARQRLKGMK ; 418: DDKEEEEDGT ; GSPRLNDR
Sequence Length	418
String	P17870
Sub Unit	Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with ADRB2 (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated at 'Tyr-737'); phosphorylation of AP2B1 at 'Tyr-737' disrupts the interaction. Interacts (dephosphorylated at Ser-412) with CLTC. Interacts with CCR2 and ADRBK1. Interacts with CRR5. Interacts with PTAFR (phosphorylated on serine residues). Interacts with CLTC and MAP2K3. Interacts with CREB1. Interacts with TRAF6. Interacts with IGF1R and MDM2. Interacts with C5AR1. Interacts with PDE4D. Interacts with SRC (via the SH3 domain and the protein kinase domain); the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with TACR1. Interacts with RAF1. Interacts with CHUK, IKBKB and MAP3K14. Interacts with DVL1; the interaction is enhanced by phosphorylation of DVL1. Interacts with DVL2; the interaction is enhanced by phosphorylation of DVL2. Interacts with IGF1R. Associates with MAP kinase p38. Part of a MAPK signaling complex consisting of TACR1, ARRB1, SRC, MAPK1 (activated) and MAPK3 (activated). Part of a MAPK signaling complex consisting of F2RL1, ARRB1, RAF1, MAPK1 (activated) and MAPK3 (activated). Interacts with GPR143.

Uniprot	P17870
Gene Name	ARRB1
Immunogen Species	Bos Taurus (Cattle)
Kegg	bta:281637
Unigene	Bt.52082

Reference	1. "Beta-arrestin: a protein that regulates beta-adrenergic receptor function." Lohse M.J., Benovic J.L., Codina J., Caron M.G., Lefkowitz R.J. Science248:1547-1550(1990) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];FUNCTION 2. "Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems." Lohse M.J., Andexinger S., Pitcher J., Trukawinski S., Codina J., Faure J.P., Caron M.G., Lefkowitz R.J. J. Biol. Chem.267:8558-8564(1992) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN BETA-ADRENERGIC RECEPTOR REGULATION 3. "Polypeptide variants of beta-arrestin and arrestin3." Sterne-Marr R., Gurevich V.V., Goldsmith P., Bodine R.C., Sanders C., Donoso L.A., Benovic J.L. J. Biol. Chem.268:15640-15648(1993) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ALTERNATIVE SPLICING tissue: Brain. 4. "Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors." Gurevich V.V., Dion S.B., Onorato J.J., Ptasienski J., Kim C.M., Sterne-Marr R., Hosey M.M., Benovic J.L. J. Biol. Chem.270:720-731(1995) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH ADRB2 AND CHRM2 5. "Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding." Gaidarov I., Krupnick J.G., Falck J.R., Benovic J.L., Keen J.H. EMBO J.18:871-881(1999) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHOINOSITIDE-BINDING 6. "A direct role for arrestins in desensitization of the luteinizing hormone/choriogonadotropin receptor in porcine ovarian follicular membranes." Mukherjee S., Palczewski K., Gurevich V.V., Benovic J.L., Banga J.P., Hunzicker-Dunn M. Proc. Natl. Acad. Sci. U.S.A.96:493-498(1999) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN DESENSITIZATION OF LHCGR 7. "Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2." Mukherjee S., Gurevich V.V., Preninger A., Hamm H.E., Bader M.-F., Fazleabas A.T., Birnbaumer L., Hunzicker-Dunn M. J. Biol. Chem.277:17916-17927(2002) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH LHCGR 8. "The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO ARF6 ELMO protein network." Bouschet T., Martin S., Kanamarlapudi V., Mundell S., Henley J.M. J. Cell Sci.120:2489-2497(2007) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: SUBCELLULAR LOCATION;INTERACTION WITH CYTH2 AND CASR 9. "Agonist-selective, receptor-specific interaction of human P2Y receptors with beta-arrestin-1 and -2." Hoffmann C., Ziegler N., Reiner S., Krasel C., Lohse M.J. J. Biol. Chem.283:30933-30941(2008) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN INTERNALIZATION OF P2Y PURINOCEPTORS;SUBCELLULAR LOCATION 10. "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation." Han M., Gurevich V.V., Vishnivetskiy S.A., Sigler P.B., Schubert C. Structure9:869-880(2001) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-393;INTERACTION WITH CHRM2 11. "Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis." Milano S.K., Pace H.C., Kim Y.-M., Brenner C., Benovic J.L. Biochemistry41:3321-3328(2002) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS);INTERACTION WITH AP2B1 AND CLTC;MUTAGENESIS OF PHE-391; ARG-395 AND LEU-396 12. "Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding." Milano S.K., Kim Y.-M., Stefano F.P., Benovic J.L., Brenner C. J. Biol. Chem.281:9812-9823(2006) [PubMed] [Europe PMC] [Abstract] [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS);SUBUNIT;INSP6-BINDING;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-157; LYS-160; ARG-161; LYS-232; ARG-236; LYS-250; LYS-324 AND LYS-326

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