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    ARR3 arrestin 3 [ Homo sapiens (human) ]

    Gene ID: 407, updated on 17-Jun-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Novel Splicing Variants in the ARR3 Gene Cause the Female-Limited Early-Onset High Myopia.

    Novel Splicing Variants in the ARR3 Gene Cause the Female-Limited Early-Onset High Myopia.
    Niu J, Zhu W, Jin X, Teng X, Zhang J., Free PMC Article

    04/4/2024
    Pathogenic variant in the X-linked ARR3 gene associated with variable early-onset myopia.

    Pathogenic variant in the X-linked ARR3 gene associated with variable early-onset myopia.
    Ediae GU, Chisholm C, Lemire G, Campbell F, Boycott KM.

    01/12/2024
    Genetic and clinical landscape of ARR3-associated MYP26: the most common cause of Mendelian early-onset high myopia with a unique inheritance.

    Genetic and clinical landscape of ARR3-associated MYP26: the most common cause of Mendelian early-onset high myopia with a unique inheritance.
    Wang Y, Xiao X, Li X, Yi Z, Jiang Y, Zhang F, Zhou L, Li S, Jia X, Sun W, Wang P, Zhang Q., Free PMC Article

    09/26/2023
    Cannabinoid 1 (CB1) receptor arrestin subtype-selectivity and phosphorylation dependence.

    Cannabinoid 1 (CB(1) ) receptor arrestin subtype-selectivity and phosphorylation dependence.
    Manning JJ, Rawcliffe G, Finlay DB, Glass M., Free PMC Article

    01/21/2023
    Early onset X-linked female limited high myopia in three multigenerational families caused by novel mutations in the ARR3 gene.

    Early onset X-linked female limited high myopia in three multigenerational families caused by novel mutations in the ARR3 gene.
    van Mazijk R, Haarman AEG, Hoefsloot LH, Polling JR, van Tienhoven M, Klaver CCW, Verhoeven VJM, Loudon SE, Thiadens AAHJ, Kievit AJA., Free PMC Article

    05/7/2022
    The Y1R is able to bind Galpha0 protein as well as arr-3 simultaneously and internalizes as a supercomplex.

    Different mode of arrestin-3 binding at the human Y(1) and Y(2) receptor.
    Wanka L, Babilon S, Kaiser A, Mörl K, Beck-Sickinger AG.

    09/21/2019
    >15-fold higher affinity for inactive JNK3 than for active JNK3; shift in the binding site following JNK3 activation

    Arrestin-3 scaffolding of the JNK3 cascade suggests a mechanism for signal amplification.
    Perry NA, Kaoud TS, Ortega OO, Kaya AI, Marcus DJ, Pleinis JM, Berndt S, Chen Q, Zhan X, Dalby KN, Lopez CF, Iverson TM, Gurevich VV., Free PMC Article

    03/16/2019
    These data highlight a novel arrestin-mediated modulation of CREB signalling, suggesting a reciprocal relationship between arrestin2 and arrestin3, wherein recruitment of arrestin3 restricts the ability of beta2AR to activate prolonged CREB phosphorylation by precluding recruitment of an arrestin2/Src/p38 complex.

    Reciprocal regulation of β(2)-adrenoceptor-activated cAMP response-element binding protein signalling by arrestin2 and arrestin3.
    Pearce A, Sanders L, Brighton PJ, Rana S, Konje JC, Willets JM.

    05/19/2018
    These data suggest that heterozygous mutations in ARR3 might be responsible for X-linked female-limited early onset high myopia in the three families, a pattern contrary to the standard X-linked recessive trait.

    X-linked heterozygous mutations in ARR3 cause female-limited early onset high myopia.
    Xiao X, Li S, Jia X, Guo X, Zhang Q., Free PMC Article

    02/3/2018
    In the cell membrane, arrestin-3 dissociates quickly and almost completely from the Beta2-adrenoceptor.

    Engineered hyperphosphorylation of the β2-adrenoceptor prolongs arrestin-3 binding and induces arrestin internalization.
    Zindel D, Butcher AJ, Al-Sabah S, Lanzerstorfer P, Weghuber J, Tobin AB, Bünemann M, Krasel C., Free PMC Article

    04/4/2015
    Identification of receptor binding-induced conformational changes in non-visual arrestins.

    Identification of receptor binding-induced conformational changes in non-visual arrestins.
    Zhuo Y, Vishnivetskiy SA, Zhan X, Gurevich VV, Klug CS., Free PMC Article

    02/14/2015
    The 25-amino acid N-domain element of arrestin 3 has the highest affinity for JNK3alpha2, suggesting that it is the key site for JNK3alpha2 docking.

    Arrestin-3 binds the MAP kinase JNK3α2 via multiple sites on both domains.
    Zhan X, Perez A, Gimenez LE, Vishnivetskiy SA, Gurevich VV., Free PMC Article

    09/27/2014
    arrestin-3 regulates the activity of multiple JNK isoforms, suggesting that it might play a role in survival and apoptosis of all cell types.

    Arrestin-dependent activation of JNK family kinases.
    Zhan X, Kook S, Gurevich EV, Gurevich VV., Free PMC Article

    04/19/2014
    These data suggest cell type- and subcellular compartment-dependent differences in GRK/arrestin-mediated desensitization and signaling.

    Distinct cellular and subcellular distributions of G protein-coupled receptor kinase and arrestin isoforms in the striatum.
    Bychkov E, Zurkovsky L, Garret MB, Ahmed MR, Gurevich EV., Free PMC Article

    04/27/2013
    Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant.

    Silent scaffolds: inhibition OF c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant.
    Breitman M, Kook S, Gimenez LE, Lizama BN, Palazzo MC, Gurevich EV, Gurevich VV., Free PMC Article

    08/25/2012
    the TGN acts as a checkpoint for both the recycling and down-regulation of beta1AR and arrestin-3 not only mediates beta1AR endocytosis but also its recycling through the TGN

    Trans-Golgi Network (TGN) as a regulatory node for β1-adrenergic receptor (β1AR) down-modulation and recycling.
    Cheng SB, Filardo EJ., Free PMC Article

    07/21/2012
    PP2A inhibits association between the Na+,K+-ATPase and arrestin, and diminishes the effect of arrestin on Na+,K+-ATPase trafficking.

    Protein phosphatase 2A interacts with the Na,K-ATPase and modulates its trafficking by inhibition of its association with arrestin.
    Kimura T, Han W, Pagel P, Nairn AC, Caplan MJ., Free PMC Article

    05/12/2012
    upon ligand activation, CysLT(1)R is tyrosine-phosphorylated and released from heterodimers with CysLT(2)R and, subsequently, internalizes from the plasma membrane to the nuclear membrane in a clathrin-, arrestin-3-, and Rab-5-dependent manner

    Ligand-induced tyrosine phosphorylation of cysteinyl leukotriene receptor 1 triggers internalization and signaling in intestinal epithelial cells.
    Parhamifar L, Sime W, Yudina Y, Vilhardt F, Mörgelin M, Sjölander A., Free PMC Article

    07/9/2011
    The agonist-induced internalization of GPR109A receptors is regulated by GRK2 and arrestin3 in a pertussis toxin-sensitive manner and that internalized receptor recycling is independent of endosomal acidification.

    Internalization of the human nicotinic acid receptor GPR109A is regulated by G(i), GRK2, and arrestin3.
    Li G, Shi Y, Huang H, Zhang Y, Wu K, Luo J, Sun Y, Lu J, Benovic JL, Zhou N., Free PMC Article

    08/9/2010
    two non-visual arrestins, arrestin2 and arrestin3, localize to the centrosome, a key organelle involved in microtubule nucleation and bipolar mitotic spindle assembly

    Non-visual arrestins are constitutively associated with the centrosome and regulate centrosome function.
    Shankar H, Michal A, Kern RC, Kang DS, Gurevich VV, Benovic JL., Free PMC Article

    04/19/2010
    the molecular interactions of arrestin2 and arrestin3 and their individual domains with the components of the two MAPK cascades, ASK1-MKK4-JNK3 and c-Raf-1-MEK1-ERK2

    How does arrestin assemble MAPKs into a signaling complex?
    Song X, Coffa S, Fu H, Gurevich VV., Free PMC Article

    01/21/2010
    Arrestin 3 but not arrestin 2 is required for internalization of C-C chemokine receptor CCR7 when bound to C-C chemokine ligand CCL19. In contrast, arrestins are not required for internalization of CCR7/CCL21.

    Arrestin 3 mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21.
    Byers MA, Calloway PA, Shannon L, Cunningham HD, Smith S, Li F, Fassold BC, Vines CM., Free PMC Article

    01/21/2010
    The light-dependent translocation of cone arrestin suggests a role in light-dark adaptation of cones.

    Identification and light-dependent translocation of a cone-specific antigen, cone arrestin, recognized by monoclonal antibody 7G6.
    Zhang H, Cuenca N, Ivanova T, Church-Kopish J, Frederick JM, MacLeish PR, Baehr W.

    01/21/2010
    Arrestin in all conformations binds JNK3 comparably, whereas Mdm2 preferentially binds cone arrestin 'frozen' in the basal state.

    Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites.
    Song X, Gurevich EV, Gurevich VV., Free PMC Article

    01/21/2010
    Regulation of arrestin-3 phosphorylation by casein kinase II.

    Regulation of arrestin-3 phosphorylation by casein kinase II.
    Kim YM, Barak LS, Caron MG, Benovic JL.

    01/21/2010
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