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Biochemistry Research International
Volume 2012 (2012), Article ID 242764, 12 pages
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 [14 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.
- 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.
- J. Horak, “Regulations of sugar transporters: insights from yeast,” Current Genetics, vol. 59, no. 1-2, pp. 1–31, 2013.
- Martin Scheffner, and Sharad Kumar, “Mammalian HECT ubiquitin-protein ligases: Biological and pathophysiological aspects,” Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2013.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.