Arrestin beta 2

Arrestin beta 2

Arrestin, beta 2, also known as ARRB2, is a human gene that codes an intracellular protein β-arrestin-2.

Members of arrestin/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of G protein-coupled receptors and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals. Arrestin beta 2, like arrestin beta 1, was shown to inhibit beta-adrenergic receptor function in vitro. It is expressed at high levels in the central nervous system and may play a role in the regulation of synaptic receptors. Besides the brain, a cDNA for arrestin beta 2 was isolated from thyroid gland, and thus it may also be involved in hormone-specific desensitization of TSH receptors. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined. [cite web | title = Entrez Gene: ARRB2 arrestin, beta 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=409| accessdate = ]

The protein may interact with the agonist DOI in 5-HT2A receptor signaling.cite journal | author = Schmid CL, Raehal KM, Bohn LM | title = Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 105 | issue = 3 | pages = 1079–84 | year = 2008 | month = January | pmid = 18195357 | pmc = 2242710 | doi = 10.1073/pnas.0708862105 | url = | issn = ] cite journal | author = Abbas A, Roth BL | title = Arresting serotonin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 105 | issue = 3 | pages = 831–2 | year = 2008 | month = January | pmid = 18195368 | pmc = 2242676 | doi = 10.1073/pnas.0711335105 | url = | issn = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lefkowitz RJ |title=G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. |journal=J. Biol. Chem. |volume=273 |issue= 30 |pages= 18677–80 |year= 1998 |pmid= 9668034 |doi=
*cite journal | author=Attramadal H, Arriza JL, Aoki C, "et al." |title=Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17882–90 |year= 1992 |pmid= 1517224 |doi=
*cite journal | author=Rapoport B, Kaufman KD, Chazenbalk GD |title=Cloning of a member of the arrestin family from a human thyroid cDNA library. |journal=Mol. Cell. Endocrinol. |volume=84 |issue= 3 |pages= R39–43 |year= 1992 |pmid= 1587386 |doi=
*cite journal | author=Calabrese G, Sallese M, Stornaiuolo A, "et al." |title=Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes. |journal=Genomics |volume=23 |issue= 1 |pages= 286–8 |year= 1995 |pmid= 7695743 |doi= 10.1006/geno.1994.1497
*cite journal | author=Parruti G, Peracchia F, Sallese M, "et al." |title=Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing. |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9753–61 |year= 1993 |pmid= 8486659 |doi=
*cite journal | author=Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J |title=Role of the Cys90, Cys95 and Cys173 residues in the structure and function of the human platelet-activating factor receptor. |journal=FEBS Lett. |volume=402 |issue= 2-3 |pages= 203–8 |year= 1997 |pmid= 9037196 |doi=
*cite journal | author=Barak LS, Ferguson SS, Zhang J, Caron MG |title=A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 27497–500 |year= 1997 |pmid= 9346876 |doi=
*cite journal | author=Laporte SA, Oakley RH, Zhang J, "et al." |title=The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 3712–7 |year= 1999 |pmid= 10097102 |doi=
*cite journal | author=Cheng ZJ, Zhao J, Sun Y, "et al." |title=beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4. |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2479–85 |year= 2000 |pmid= 10644702 |doi=
*cite journal | author=Lin F, Wang H, Malbon CC |title=Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization. |journal=J. Biol. Chem. |volume=275 |issue= 25 |pages= 19025–34 |year= 2000 |pmid= 10858453 |doi=
*cite journal | author=McDonald PH, Chow CW, Miller WE, "et al." |title=Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3. |journal=Science |volume=290 |issue= 5496 |pages= 1574–7 |year= 2000 |pmid= 11090355 |doi=
*cite journal | author=Luttrell LM, Roudabush FL, Choy EW, "et al." |title=Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 5 |pages= 2449–54 |year= 2001 |pmid= 11226259 |doi= 10.1073/pnas.041604898
*cite journal | author=Cen B, Yu Q, Guo J, "et al." |title=Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor. |journal=J. Neurochem. |volume=76 |issue= 6 |pages= 1887–94 |year= 2001 |pmid= 11259507 |doi=
*cite journal | author=Oakley RH, Laporte SA, Holt JA, "et al." |title=Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19452–60 |year= 2001 |pmid= 11279203 |doi= 10.1074/jbc.M101450200
*cite journal | author=Miller WE, McDonald PH, Cai SF, "et al." |title=Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 27770–7 |year= 2001 |pmid= 11356842 |doi= 10.1074/jbc.M102264200
*cite journal | author=Claing A, Chen W, Miller WE, "et al." |title=beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42509–13 |year= 2001 |pmid= 11533043 |doi= 10.1074/jbc.M108399200
*cite journal | author=Hilairet S, Bélanger C, Bertrand J, "et al." |title=Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42182–90 |year= 2001 |pmid= 11535606 |doi= 10.1074/jbc.M107323200
*cite journal | author=Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ |title=Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin. |journal=Science |volume=294 |issue= 5545 |pages= 1307–13 |year= 2001 |pmid= 11588219 |doi= 10.1126/science.1063866
*cite journal | author=Chen Z, Dupré DJ, Le Gouill C, "et al." |title=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. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7356–62 |year= 2002 |pmid= 11729201 |doi= 10.1074/jbc.M110058200

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = no
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем решить контрольную работу

Look at other dictionaries:

  • Arrestin beta 1 — Arrestin, beta 1, also known as ARRB1, is a human gene. [cite web | title = Entrez Gene: ARRB1 arrestin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView TermToSearch=408| accessdate = ] PBB Summary section title …   Wikipedia

  • Arrestin — protein Name = arrestin beta 1 caption = width = HGNCid = 711 Symbol = ARRB1 AltSymbols = ARR1 EntrezGene = 408 OMIM = 107940 RefSeq = NM 004041 UniProt = P49407 PDB = ECnumber = Chromosome = 11 Arm = q Band = 13 LocusSupplementaryData = protein… …   Wikipedia

  • Beta adrenergic receptor kinase — (BARK) is a serine/threonine intracellular kinase. It is activated by PKA and its target is the beta adrenergic receptor. It is one method by which the cell will desensitize itself from epinephrine overstimulation.Pippig S, et al. Overexpression… …   Wikipedia

  • Beta gamma crystallin — Beta/Gamma crystallin Identifiers Symbol Crystall Pfam PF00030 InterPro …   Wikipedia

  • Beta adrenergic receptor kinase-2 — Adrenergic, beta, receptor kinase 2, also known as ADRBK2, is a human gene. PBB Summary section title = summary text = The beta adrenergic receptor kinase specifically phosphorylates the agonist occupied form of the beta adrenergic and related G… …   Wikipedia

  • Beta-1 adrenergic receptor — The beta 1 adrenergic receptor (β1 adrenoreceptor), also known as ADRB1, is an beta adrenergic receptor, and also denotes the human gene encoding it.ReceptorActionsActions of the β1 receptor include: *stimulate viscous, amylase filled secretions… …   Wikipedia

  • Crystallin, beta A1 — Identifiers Symbols CRYBA1; CRYB1 External IDs OMIM:  …   Wikipedia

  • SAG (gene) — S antigen; retina and pineal gland (arrestin), also known as SAG, is a human gene.cite web | title = Entrez Gene: SAG S antigen; retina and pineal gland (arrestin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene Cmd=ShowDetailView… …   Wikipedia

  • Mdm2 — p53 binding protein homolog (mouse) Solution structure of Mdm2. [1] …   Wikipedia

  • 5-HT2A receptor — The mammalian 5 HT2A receptor is a subtype of the 5 HT2 receptor which belongs to the serotonin receptor family and is a G protein coupled receptor (GPCR).cite journal | author = Cook EH, Fletcher KE, Wainwright M, Marks N, Yan SY, Leventhal BL | …   Wikipedia

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”