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Biochemistry Research International
Volume 2012 (2012), Article ID 242764, 12 pages
http://dx.doi.org/10.1155/2012/242764
Review Article

Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family

1Institut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75205 Paris, France
2Instituto de Investigaciones Biomédicas, CSIC-UAM, Arturo Duperier, 4, 28029 Madrid, Spain

Received 1 June 2012; Accepted 28 July 2012

Academic Editor: Dmitry Karpov

Copyright © 2012 Michel Becuwe et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Citations to this Article [33 citations]

The following is the list of published articles that have cited the current article.

  • Fortune F. Shea, Jennie L. Rowell, Yechaowei Li, Tien-Hsien Chang, and Carlos E. Alvarez, “Mammalian Alpha Arrestins Link Activated Seven Transmembrane Receptors to Nedd4 Family E3 Ubiquitin Ligases and Interact with Beta Arrestins,” Plos One, vol. 7, no. 12, 2012. View at Publisher · View at Google Scholar
  • Nobumasa Takasugi, Tomoki Sasaki, Ihori Ebinuma, Satoko Osawa, Hayato Isshiki, Koji Takeo, Taisuke Tomita, and Takeshi Iwatsubo, “FTY720/Fingolimod, a Sphingosine Analogue, Reduces Amyloid-β Production in Neurons,” PLoS ONE, vol. 8, no. 5, 2013. View at Publisher · View at Google Scholar
  • J. Horak, “Regulations of sugar transporters: insights from yeast,” Current Genetics, vol. 59, no. 1-2, pp. 1–31, 2013. View at Publisher · View at Google Scholar
  • Martin Scheffner, and Sharad Kumar, “Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects,” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013. View at Publisher · View at Google Scholar
  • Werner C Jaeger, Ruth M Seeber, Karin A Eidne, and Kevin D G Pfleger, “Molecular determinants of orexin receptor-arrestin-ubiquitin complex formation,” British Journal of Pharmacology, vol. 171, no. 2, pp. 364–374, 2013. View at Publisher · View at Google Scholar
  • Patricia Chastagner, Loredana Puca, Christel Brou, Vannary Meas-Yedid, and Alain Israel, “alpha-arrestin 1 (ARRDC1) and beta-arrestins cooperate to mediate Notch degradation in mammals,” Journal Of Cell Science, vol. 126, no. 19, pp. 4457–4468, 2013. View at Publisher · View at Google Scholar
  • Satoshi Uemura, Fumiyoshi Abe, Asaha Suzuki, Takahiro Mochizuki, and Toshiki Hiraki, “Pressure-Induced Endocytic Degradation of the Saccharomyces cerevisiae Low-Affinity Tryptophan Permease Tat1 Is Mediated by Rsp5 Ubiquitin Ligase and Functionally Redundant PPxY Motif Proteins,” Eukaryotic Cell, vol. 12, no. 7, pp. 990–997, 2013. View at Publisher · View at Google Scholar
  • Bruno André, Ahmad Merhi, and Myriam Crapeau, “Stress conditions promote yeast Gap1 permease ubiquitylation and down-regulation via the arrestin-like bul and aly proteins,” Journal of Biological Chemistry, vol. 289, no. 32, pp. 22103–22116, 2014. View at Publisher · View at Google Scholar
  • Christopher G. Alvaro, Allyson F. O'Donnell, Derek C. Prosser, Andrew A. Augustine, Aaron Goldman, Jeffrey L. Brodsky, Martha S. Cyert, Beverly Wendland, and Jeremy Thorner, “Specific alpha-Arrestins Negatively Regulate Saccharomyces cerevisiae Pheromone Response by Down-Modulating the G-Protein-Coupled Receptor Ste2,” Molecular and Cellular Biology, vol. 34, no. 14, pp. 2660–2681, 2014. View at Publisher · View at Google Scholar
  • Pirjo M. Apaja, and Gergely L. Lukacs, “Protein homeostasis at the plasma membrane,” Physiology, vol. 29, no. 4, pp. 265–277, 2014. View at Publisher · View at Google Scholar
  • Loredana Puca, and Christel Brou, “alpha-Arrestins - new players in Notch and GPCR signaling pathways in mammals,” Journal of Cell Science, vol. 127, no. 7, pp. 1359–1367, 2014. View at Publisher · View at Google Scholar
  • Dong Soo Kang, Xufan Tian, and Jeffrey L Benovic, “Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking,” Current Opinion in Cell Biology, vol. 27, pp. 63–71, 2014. View at Publisher · View at Google Scholar
  • M. Babst, “Quality control: Quality control at the plasma membrane: One mechanism does not fit all,” The Journal of Cell Biology, vol. 205, no. 1, pp. 11–20, 2014. View at Publisher · View at Google Scholar
  • Christian Schuberth, and Roland Wedlich-Söldner, “Building a patchwork – the yeast plasma membrane as model to study lateral domain formation,” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014. View at Publisher · View at Google Scholar
  • Zongtian Tong, Min-Sik Kim, Akhilesh Pandey, and Peter J. Espenshade, “Identification of candidate substrates for the golgi tul1 E3 ligase using quantitative diGly proteomics in yeast,” Molecular and Cellular Proteomics, vol. 13, no. 11, pp. 2871–2882, 2014. View at Publisher · View at Google Scholar
  • Michel Becuwe, and Sébastien Léon, “Integrated control of transporter endocytosis and recycling by the arrestin-related protein Rod1 and the ubiquitin ligase Rsp5,” eLife, vol. 3, 2014. View at Publisher · View at Google Scholar
  • Kassem Ghaddar, Ahmad Merhi, Elie Saliba, Eva-Maria Krammer, Martine Prévost, and Bruno André, “Substrate-induced ubiquitylation and endocytosis of yeast amino acid permeases,” Molecular and Cellular Biology, vol. 34, no. 24, pp. 4447–4463, 2014. View at Publisher · View at Google Scholar
  • Grégory Vert, and Christian Luschnig, “The dynamics of plant plasma membrane proteins: PINs and beyond,” Development (Cambridge), vol. 141, no. 15, pp. 2924–2938, 2014. View at Publisher · View at Google Scholar
  • Réjane Pratelli, and Guillaume Pilot, “Regulation of amino acid metabolic enzymes and transporters in plants,” Journal of Experimental Botany, vol. 65, no. 19, pp. 5535–5556, 2014. View at Publisher · View at Google Scholar
  • Pilar Puig-Sarries, Marie-Jose Bijlmakers, Alice Zuin, Anne Bichmann, Miquel Pons, and Bernat Crosas, “An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination,” Biochemical Journal, vol. 469, pp. 455–467, 2015. View at Publisher · View at Google Scholar
  • H.M. Gaudet, S.B. Cheng, E.M. Christensen, and E.J. Filardo, “The G-protein coupled estrogen receptor, GPER: The inside and inside-out story,” Molecular and Cellular Endocrinology, 2015. View at Publisher · View at Google Scholar
  • Wenjing Li, Hong Zhu, Xuelian Zhao, Deborah Brancho, Yuanxin Liang, Yiyu Zou, Craig Bennett, and Chi-Wing Chow, “Dysregulated Inflammatory Signaling upon Charcot-Marie-Tooth Type 1C Mutation of SIMPLE Protein,” Molecular And Cellular Biology, vol. 35, no. 14, pp. 2464–2478, 2015. View at Publisher · View at Google Scholar
  • Huiwen Hu, Chengyong Tang, Qinghu Jiang, Wei Luo, Jiming Liu, Xufu Wei, Rui Liu, and Zhongjun Wu, “Reduced ubiquitin-specific protease 9X expression induced by RNA interference inhibits the bioactivity of hepatocellular carcinoma cells,” Oncology Letters, vol. 10, no. 1, pp. 268–272, 2015. View at Publisher · View at Google Scholar
  • A. Herrador, D. Livas, L. Soletto, M. Becuwe, S. Leon, and O. Vincent, “Casein kinase 1 controls the activation threshold of an  -arrestin by multisite phosphorylation of the interdomain hinge,” Molecular Biology of the Cell, vol. 26, no. 11, pp. 2128–2138, 2015. View at Publisher · View at Google Scholar
  • Derek C. Prosser, Anthony E. Pannunzio, Jeffrey L. Brodsky, Jeremy Thorner, Beverly Wendland, and Allyson F. O'Donnell, “alpha-Arrestins participate in cargo selection for both clathrin-independent and clathrin-mediated endocytosis,” Journal Of Cell Science, vol. 128, no. 22, pp. 4220–4234, 2015. View at Publisher · View at Google Scholar
  • Kamila Skieterska, Ao Shen, Dorien Clarisse, Pieter Rondou, Dasiel Oscar Borroto-Escuela, Béatrice Lintermans, Kjell Fuxe, Yang Kevin Xiang, and Kathleen Van Craenenbroeck, “Characterization of the interaction between the dopamine D4 receptor, KLHL12 and β-arrestins,” Cellular Signalling, 2016. View at Publisher · View at Google Scholar
  • Ignacio Ibáñez, F. Javier Díez-Guerra, Cecilio Giménez, and Francisco Zafra, “Activity dependent internalization of the glutamate transporter GLT-1 mediated by β-arrestin 1 and ubiquitination,” Neuropharmacology, 2016. View at Publisher · View at Google Scholar
  • E. L. Guiney, T. Klecker, and S. D. Emr, “Identification of the endocytic sorting signal recognized by the Art1-Rsp5 ubiquitin ligase complex,” Molecular Biology of the Cell, vol. 27, no. 25, pp. 4043–4054, 2016. View at Publisher · View at Google Scholar
  • Jun Meng, Zhenyu Yao, Yaqing He, Renli Zhang, Yanwei Zhang, Xiangjie Yao, Hong Yang, Long Chen, Zhen Zhang, Hailong Zhang, Xueqin Bao, Gang Hu, Tangchun Wu, and Jinquan Cheng, “ARRDC4 regulates enterovirus 71-induced innate immune response by promoting K63 polyubiquitination of MDA5 through TRIM65,” Cell Death and Disease, vol. 8, no. 6, pp. e2866, 2017. View at Publisher · View at Google Scholar
  • Junie Hovsepian, Quentin Defenouillère, Véronique Albanèse, Libuše Váchová, Camille Garcia, Zdena Palková, and Sébastien Léon, “Multilevel regulation of an α-arrestin by glucose depletion controls hexose transporter endocytosis,” The Journal of Cell Biology, pp. jcb.201610094, 2017. View at Publisher · View at Google Scholar
  • Kamila Skieterska, Pieter Rondou, and Kathleen Van Craenenbroeck, “Regulation of G Protein-Coupled Receptors by Ubiquitination,” International Journal of Molecular Sciences, vol. 18, no. 5, pp. 923, 2017. View at Publisher · View at Google Scholar
  • Hsuan-Chung Ho, Jason A. MacGurn, and Scott D. Emr, “Deubiquitinating enzymes Ubp2 and Ubp15 regulate endocytosis by limiting ubiquitination and degradation of ARTs,” Molecular Biology of the Cell, vol. 28, no. 9, pp. 1271–1283, 2017. View at Publisher · View at Google Scholar
  • Jorge L. Sarmiento-Villamil, Nicolás E. García-Pedrajas, Lourdes Baeza-Montañez, and María D. García-Pedrajas, “ The APSES transcription factor Vst1 is a key regulator of development in microsclerotium- and resting mycelium-producing Verticillium species ,” Molecular Plant Pathology, 2017. View at Publisher · View at Google Scholar