Arrestin beta 2: Difference between revisions

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{{Infobox_gene}}
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'''Beta-arrestin-2''', also known as '''arrestin beta-2''', is an intracellular [[protein]] that in humans is encoded by the ''ARRB2'' [[gene]].
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| update_protein_box = yes
| update_summary = no
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Members of [[arrestin]]/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of [[G protein-coupled receptor]]s and cause specific dampening of cellular responses to stimuli such as hormones, neurotransmitters, or sensory signals,<ref name="pmid18622177">{{cite journal | vauthors = Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK | title = Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice | journal = Behavioural Pharmacology | volume = 19 | issue = 4 | pages = 298–307 | date = July 2008 | pmid = 18622177 | pmc = 2751575 | doi = 10.1097/FBP.0b013e328308f1e6 }}</ref><ref name="pmid19399231">{{cite journal | vauthors = Li Y, Liu X, Liu C, Kang J, Yang J, Pei G, Wu C | title = Improvement of morphine-mediated analgesia by inhibition of β-arrestin2 expression in mice periaqueductal gray matter | journal = International Journal of Molecular Sciences | volume = 10 | issue = 3 | pages = 954–63 | date = March 2009 | pmid = 19399231 | pmc = 2672012 | doi = 10.3390/ijms10030954 }}</ref><ref name="pmid17947509">{{cite journal | vauthors = Zheng H, Loh HH, Law PY |authorlink2=Harold Loh| title = Beta-arrestin-dependent mu-opioid receptor-activated extracellular signal-regulated kinases (ERKs) Translocate to Nucleus in Contrast to G protein-dependent ERK activation | journal = Molecular Pharmacology | volume = 73 | issue = 1 | pages = 178–90 | date = January 2008 | pmid = 17947509 | pmc = 2253657 | doi = 10.1124/mol.107.039842 }}</ref> as well as having signalling roles in their own right.<ref name="pmid17215450">{{cite journal | vauthors = Ma L, Pei G | title = Beta-arrestin signaling and regulation of transcription | journal = Journal of Cell Science | volume = 120 | issue = Pt 2 | pages = 213–8 | date = January 2007 | pmid = 17215450 | doi = 10.1242/jcs.03338 }}</ref><ref name="pmid18037927">{{cite journal | vauthors = Defea K | title = Beta-arrestins and heterotrimeric G-proteins: collaborators and competitors in signal transduction | journal = British Journal of Pharmacology | volume = 153 Suppl 1 | issue = S1 | pages = S298-309 | date = March 2008 | pmid = 18037927 | pmc = 2268080 | doi = 10.1038/sj.bjp.0707508 }}</ref><ref name="pmid18268361">{{cite journal | vauthors = Barki-Harrington L, Rockman HA | title = Beta-arrestins: multifunctional cellular mediators | journal = Physiology | volume = 23 | issue =  | pages = 17–22 | date = February 2008 | pmid = 18268361 | doi = 10.1152/physiol.00042.2007 }}</ref><ref name="pmid19103204">{{cite journal | vauthors = Patel PA, Tilley DG, Rockman HA | title = Physiologic and cardiac roles of beta-arrestins | journal = Journal of Molecular and Cellular Cardiology | volume = 46 | issue = 3 | pages = 300–8 | date = March 2009 | pmid = 19103204 | doi = 10.1016/j.yjmcc.2008.11.015 }}</ref><ref name="pmid19442183">{{cite journal | vauthors = Golan M, Schreiber G, Avissar S | title = Antidepressants, beta-arrestins and GRKs: from regulation of signal desensitization to intracellular multifunctional adaptor functions | journal = Current Pharmaceutical Design | volume = 15 | issue = 14 | pages = 1699–708 | year = 2009 | pmid = 19442183 | doi = 10.2174/138161209788168038 }}</ref> 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 receptor]]s. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.<ref>{{cite web | title = Entrez Gene: ARRB2 arrestin, beta 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=409| accessdate = }}</ref>
{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Arrestin, beta 2
| HGNCid = 712
| Symbol = ARRB2
| AltSymbols =; ARB2; ARR2; DKFZp686L0365
| OMIM = 107941
| ECnumber =
| Homologene = 3183
| MGIid = 99474
| GeneAtlas_image1 = PBB_GE_ARRB2_203388_at_tn.png
| Function =  
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}  
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007600 |text = sensory perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 409
    | Hs_Ensembl = ENSG00000141480
    | Hs_RefseqProtein = NP_004304
    | Hs_RefseqmRNA = NM_004313
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 4560533
    | Hs_GenLoc_end = 4571544
    | Hs_Uniprot = P32121
    | Mm_EntrezGene = 216869
    | Mm_Ensembl = ENSMUSG00000060216
    | Mm_RefseqmRNA = XM_993633
    | Mm_RefseqProtein = XP_998727
    | Mm_GenLoc_db =
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 70248840
    | Mm_GenLoc_end = 70257023
    | Mm_Uniprot = Q3UCU5
  }}
}}
'''Arrestin, beta 2''', also known as '''ARRB2''', is a human [[gene]].


Members of [[arrestin]]/beta-arrestin protein family are thought to participate in agonist-mediated desensitization of [[G protein-coupled receptor]]s 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 receptor]]s. Multiple alternatively spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been defined.<ref>{{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 = }}</ref>
The protein may interact with the agonist [[2,5-Dimethoxy-4-iodoamphetamine|DOI]] in [[5-HT2A receptor|5-HT<sub>2A</sub> receptor]] signaling.<ref name="pmid18195357">{{cite journal | vauthors = Schmid CL, Raehal KM, Bohn LM | title = Agonist-directed signaling of the serotonin 2A receptor depends on beta-arrestin-2 interactions in vivo | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 3 | pages = 1079–84 | date = January 2008 | pmid = 18195357 | pmc = 2242710 | doi = 10.1073/pnas.0708862105 }}</ref><ref name="pmid18195368">{{cite journal | vauthors = Abbas A, Roth BL | title = Arresting serotonin | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 105 | issue = 3 | pages = 831–2 | date = January 2008 | pmid = 18195368 | pmc = 2242676 | doi = 10.1073/pnas.0711335105 }}</ref>


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
Arrestin beta 2 has been shown to [[Protein-protein interaction|interact]] with
*  [[AP2B1]],<ref name="pmid10097102">{{cite journal | vauthors = Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS | title = The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 7 | pages = 3712–7 | date = March 1999 | pmid = 10097102 | pmc = 22359 | doi = 10.1073/pnas.96.7.3712 }}</ref><ref name="pmid12070169">{{cite journal | vauthors = Kim YM, Benovic JL | title = Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking | journal = The Journal of Biological Chemistry | volume = 277 | issue = 34 | pages = 30760–8 | date = August 2002 | pmid = 12070169 | doi = 10.1074/jbc.M204528200 }}</ref>
* [[PSCD2]],<ref name="pmid11533043">{{cite journal | vauthors = Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ | title = beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis | journal = The Journal of Biological Chemistry | volume = 276 | issue = 45 | pages = 42509–13 | date = November 2001 | pmid = 11533043 | doi = 10.1074/jbc.M108399200 }}</ref>
* [[Mdm2]],<ref name="pmid12488444">{{cite journal | vauthors = Wang P, Gao H, Ni Y, Wang B, Wu Y, Ji L, Qin L, Ma L, Pei G | title = Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2 | journal = The Journal of Biological Chemistry | volume = 278 | issue = 8 | pages = 6363–70 | date = February 2003 | pmid = 12488444 | doi = 10.1074/jbc.M210350200 }}</ref><ref name="pmid12538596">{{cite journal | vauthors = Wang P, Wu Y, Ge X, Ma L, Pei G | title = Subcellular localization of beta-arrestins is determined by their intact N domain and the nuclear export signal at the C terminus | journal = The Journal of Biological Chemistry | volume = 278 | issue = 13 | pages = 11648–53 | date = March 2003 | pmid = 12538596 | doi = 10.1074/jbc.M208109200 }}</ref><ref name="pmid18544533">{{cite journal | vauthors = Shenoy SK, Xiao K, Venkataramanan V, Snyder PM, Freedman NJ, Weissman AM | title = Nedd4 mediates agonist-dependent ubiquitination, lysosomal targeting, and degradation of the beta2-adrenergic receptor | journal = The Journal of Biological Chemistry | volume = 283 | issue = 32 | pages = 22166–76 | date = August 2008 | pmid = 18544533 | pmc = 2494938 | doi = 10.1074/jbc.M709668200 }}</ref> and
* [[RALGDS]].<ref name="pmid12105416">{{cite journal | vauthors = Bhattacharya M, Anborgh PH, Babwah AV, Dale LB, Dobransky T, Benovic JL, Feldman RD, Verdi JM, Rylett RJ, Ferguson SS | title = Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization | journal = Nature Cell Biology | volume = 4 | issue = 8 | pages = 547–55 | date = August 2002 | pmid = 12105416 | doi = 10.1038/ncb821 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lefkowitz RJ | title = G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization | journal = The Journal of Biological Chemistry | volume = 273 | issue = 30 | pages = 18677–80 | date = July 1998 | pmid = 9668034 | doi = 10.1074/jbc.273.30.18677 }}
| citations =
* {{cite journal | vauthors = Attramadal H, Arriza JL, Aoki C, Dawson TM, Codina J, Kwatra MM, Snyder SH, Caron MG, Lefkowitz RJ | title = Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family | journal = The Journal of Biological Chemistry | volume = 267 | issue = 25 | pages = 17882–90 | date = September 1992 | pmid = 1517224 | doi =  }}
*{{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 | vauthors = Rapoport B, Kaufman KD, Chazenbalk GD | title = Cloning of a member of the arrestin family from a human thyroid cDNA library | journal = Molecular and Cellular Endocrinology | volume = 84 | issue = 3 | pages = R39-43 | date = April 1992 | pmid = 1587386 | doi = 10.1016/0303-7207(92)90038-8 }}
*{{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 | vauthors = Calabrese G, Sallese M, Stornaiuolo A, Stuppia L, Palka G, De Blasi A | 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 | date = September 1994 | pmid = 7695743 | doi = 10.1006/geno.1994.1497 }}
*{{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 | vauthors = Parruti G, Peracchia F, Sallese M, Ambrosini G, Masini M, Rotilio D, De Blasi A | title = Molecular analysis of human beta-arrestin-1: cloning, tissue distribution, and regulation of expression. Identification of two isoforms generated by alternative splicing | journal = The Journal of Biological Chemistry | volume = 268 | issue = 13 | pages = 9753–61 | date = May 1993 | pmid = 8486659 | 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 | vauthors = 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 Letters | volume = 402 | issue = 2-3 | pages = 203–8 | date = February 1997 | pmid = 9037196 | doi = 10.1016/S0014-5793(96)01531-1 }}
*{{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 | vauthors = Barak LS, Ferguson SS, Zhang J, Caron MG | title = A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 44 | pages = 27497–500 | date = October 1997 | pmid = 9346876 | doi = 10.1074/jbc.272.44.27497 }}
*{{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 | vauthors = Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SS, Caron MG, Barak LS | title = The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 96 | issue = 7 | pages = 3712–7 | date = March 1999 | pmid = 10097102 | pmc = 22359 | doi = 10.1073/pnas.96.7.3712 }}
*{{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 | vauthors = Cheng ZJ, Zhao J, Sun Y, Hu W, Wu YL, Cen B, Wu GX, Pei G | 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 = The Journal of Biological Chemistry | volume = 275 | issue = 4 | pages = 2479–85 | date = January 2000 | pmid = 10644702 | doi = 10.1074/jbc.275.4.2479 }}
*{{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 | vauthors = Lin F, ((Wang Hy)), Malbon CC | title = Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization | journal = The Journal of Biological Chemistry | volume = 275 | issue = 25 | pages = 19025–34 | date = June 2000 | pmid = 10858453 | doi = 10.1074/jbc.275.25.19025 }}
*{{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 | vauthors = McDonald PH, Chow CW, Miller WE, Laporte SA, Field ME, Lin FT, Davis RJ, Lefkowitz RJ | title = Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3 | journal = Science | volume = 290 | issue = 5496 | pages = 1574–7 | date = November 2000 | pmid = 11090355 | doi = 10.1126/science.290.5496.1574 }}
*{{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 | vauthors = Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ | title = Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 5 | pages = 2449–54 | date = February 2001 | pmid = 11226259 | pmc = 30158 | doi = 10.1073/pnas.041604898 }}
*{{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 | vauthors = Cen B, Yu Q, Guo J, Wu Y, Ling K, Cheng Z, Ma L, Pei G | title = Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor | journal = Journal of Neurochemistry | volume = 76 | issue = 6 | pages = 1887–94 | date = March 2001 | pmid = 11259507 | doi = 10.1046/j.1471-4159.2001.00204.x }}
*{{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 | vauthors = Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG | title = Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis* | journal = The Journal of Biological Chemistry | volume = 276 | issue = 22 | pages = 19452–60 | date = June 2001 | pmid = 11279203 | doi = 10.1074/jbc.M101450200 }}
*{{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 | vauthors = Miller WE, McDonald PH, Cai SF, Field ME, Davis RJ, Lefkowitz RJ | title = Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3 | journal = The Journal of Biological Chemistry | volume = 276 | issue = 30 | pages = 27770–7 | date = July 2001 | pmid = 11356842 | doi = 10.1074/jbc.M102264200 }}
*{{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 | vauthors = Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ | title = beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis | journal = The Journal of Biological Chemistry | volume = 276 | issue = 45 | pages = 42509–13 | date = November 2001 | pmid = 11533043 | doi = 10.1074/jbc.M108399200 }}
*{{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 | vauthors = Hilairet S, Bélanger C, Bertrand J, Laperrière A, Foord SM, Bouvier M | title = Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin | journal = The Journal of Biological Chemistry | volume = 276 | issue = 45 | pages = 42182–90 | date = November 2001 | pmid = 11535606 | doi = 10.1074/jbc.M107323200 }}
*{{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 | vauthors = 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 | date = November 2001 | pmid = 11588219 | doi = 10.1126/science.1063866 }}
*{{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 | vauthors = Chen Z, Dupré DJ, Le Gouill C, Rola-Pleszczynski M, Stanková J | 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 = The Journal of Biological Chemistry | volume = 277 | issue = 9 | pages = 7356–62 | date = March 2002 | pmid = 11729201 | doi = 10.1074/jbc.M110058200 }}
*{{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 }}
}}
{{refend}}
{{refend}}


==External links==
* {{UCSC gene info|ARRB2}}
{{NLM content}}
{{NLM content}}
{{protein-stub}}
 
 
{{Membrane proteins}}
 
[[Category:Genes]]
[[Category:Human proteins]]

Latest revision as of 17:41, 5 December 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Beta-arrestin-2, also known as arrestin beta-2, is an intracellular protein that in humans is encoded by the ARRB2 gene.

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,[1][2][3] as well as having signalling roles in their own right.[4][5][6][7][8] 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.[9]

The protein may interact with the agonist DOI in 5-HT2A receptor signaling.[10][11]

Interactions

Arrestin beta 2 has been shown to interact with

References

  1. Breivogel CS, Lambert JM, Gerfin S, Huffman JW, Razdan RK (July 2008). "Sensitivity to delta9-tetrahydrocannabinol is selectively enhanced in beta-arrestin2 -/- mice". Behavioural Pharmacology. 19 (4): 298–307. doi:10.1097/FBP.0b013e328308f1e6. PMC 2751575. PMID 18622177.
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Further reading

  • Lefkowitz RJ (July 1998). "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): 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 (September 1992). "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family". The Journal of Biological Chemistry. 267 (25): 17882–90. PMID 1517224.
  • Rapoport B, Kaufman KD, Chazenbalk GD (April 1992). "Cloning of a member of the arrestin family from a human thyroid cDNA library". Molecular and Cellular Endocrinology. 84 (3): 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 (September 1994). "Chromosome mapping of the human arrestin (SAG), beta-arrestin 2 (ARRB2), and beta-adrenergic receptor kinase 2 (ADRBK2) genes". Genomics. 23 (1): 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 (May 1993). "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): 9753–61. PMID 8486659.
  • Le Gouill C, Parent JL, Rola-Pleszczynski M, Stanková J (February 1997). "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): 203–8. doi:10.1016/S0014-5793(96)01531-1. PMID 9037196.
  • Barak LS, Ferguson SS, Zhang J, Caron MG (October 1997). "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation". The Journal of Biological Chemistry. 272 (44): 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 (March 1999). "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): 3712–7. 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 (January 2000). "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): 2479–85. doi:10.1074/jbc.275.4.2479. PMID 10644702.
  • Lin F, Wang Hy, Malbon CC (June 2000). "Gravin-mediated formation of signaling complexes in beta 2-adrenergic receptor desensitization and resensitization". The Journal of Biological Chemistry. 275 (25): 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 (November 2000). "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3". Science. 290 (5496): 1574–7. doi:10.1126/science.290.5496.1574. PMID 11090355.
  • Luttrell LM, Roudabush FL, Choy EW, Miller WE, Field ME, Pierce KL, Lefkowitz RJ (February 2001). "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): 2449–54. 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 (March 2001). "Direct binding of beta-arrestins to two distinct intracellular domains of the delta opioid receptor". Journal of Neurochemistry. 76 (6): 1887–94. doi:10.1046/j.1471-4159.2001.00204.x. PMID 11259507.
  • Oakley RH, Laporte SA, Holt JA, Barak LS, Caron MG (June 2001). "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): 19452–60. doi:10.1074/jbc.M101450200. PMID 11279203.
  • Miller WE, McDonald PH, Cai SF, Field ME, Davis RJ, Lefkowitz RJ (July 2001). "Identification of a motif in the carboxyl terminus of beta -arrestin2 responsible for activation of JNK3". The Journal of Biological Chemistry. 276 (30): 27770–7. doi:10.1074/jbc.M102264200. PMID 11356842.
  • Claing A, Chen W, Miller WE, Vitale N, Moss J, Premont RT, Lefkowitz RJ (November 2001). "beta-Arrestin-mediated ADP-ribosylation factor 6 activation and beta 2-adrenergic receptor endocytosis". The Journal of Biological Chemistry. 276 (45): 42509–13. doi:10.1074/jbc.M108399200. PMID 11533043.
  • Hilairet S, Bélanger C, Bertrand J, Laperrière A, Foord SM, Bouvier M (November 2001). "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): 42182–90. doi:10.1074/jbc.M107323200. PMID 11535606.
  • Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ (November 2001). "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin". Science. 294 (5545): 1307–13. doi:10.1126/science.1063866. PMID 11588219.
  • Chen Z, Dupré DJ, Le Gouill C, Rola-Pleszczynski M, Stanková J (March 2002). "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): 7356–62. doi:10.1074/jbc.M110058200. PMID 11729201.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.