Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family
In metazoans, proteins of the arrestin family are key players of G-protein-coupled receptors (GPCRS) signaling and trafficking. Following stimulation, activated receptors are phosphorylated, thus allowing the binding of arrestins and hence an “arrest” of receptor signaling. Arrestins act by uncoupli...
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| Format: | Article |
| Language: | English |
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Wiley
2012-01-01
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| Series: | Biochemistry Research International |
| Online Access: | http://dx.doi.org/10.1155/2012/242764 |
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| author | Michel Becuwe Antonio Herrador Rosine Haguenauer-Tsapis Olivier Vincent Sébastien Léon |
| author_facet | Michel Becuwe Antonio Herrador Rosine Haguenauer-Tsapis Olivier Vincent Sébastien Léon |
| author_sort | Michel Becuwe |
| collection | DOAJ |
| description | In metazoans, proteins of the arrestin family are key players of G-protein-coupled receptors (GPCRS) signaling and trafficking. Following stimulation, activated receptors are phosphorylated, thus allowing the binding of arrestins and hence an “arrest” of receptor signaling. Arrestins act by uncoupling receptors from G proteins and contribute to the recruitment of endocytic proteins, such as clathrin, to direct receptor trafficking into the endocytic pathway. Arrestins also serve as adaptor proteins by promoting the recruitment of ubiquitin ligases and participate in the agonist-induced ubiquitylation of receptors, known to have impact on their subcellular localization and stability. Recently, the arrestin family has expanded following the discovery of arrestin-related proteins in other eukaryotes such as yeasts or fungi. Surprisingly, most of these proteins are also involved in the ubiquitylation and endocytosis of plasma membrane proteins, thus suggesting that the role of arrestins as ubiquitin ligase adaptors is at the core of these proteins' functions. Importantly, arrestins are themselves ubiquitylated, and this modification is crucial for their function. In this paper, we discuss recent data on the intricate connections between arrestins and the ubiquitin pathway in the control of endocytosis. |
| format | Article |
| id | doaj-art-23d8a85863704d4db0018a93687897aa |
| institution | OA Journals |
| issn | 2090-2247 2090-2255 |
| language | English |
| publishDate | 2012-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Biochemistry Research International |
| spelling | doaj-art-23d8a85863704d4db0018a93687897aa2025-08-20T02:04:15ZengWileyBiochemistry Research International2090-22472090-22552012-01-01201210.1155/2012/242764242764Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin FamilyMichel Becuwe0Antonio Herrador1Rosine Haguenauer-Tsapis2Olivier Vincent3Sébastien Léon4Institut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75205 Paris, FranceInstituto de Investigaciones Biomédicas, CSIC-UAM, Arturo Duperier, 4, 28029 Madrid, SpainInstitut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75205 Paris, FranceInstituto de Investigaciones Biomédicas, CSIC-UAM, Arturo Duperier, 4, 28029 Madrid, SpainInstitut Jacques Monod, Centre National de la Recherche Scientifique, UMR 7592, Université Paris Diderot, Sorbonne Paris Cité, 75205 Paris, FranceIn metazoans, proteins of the arrestin family are key players of G-protein-coupled receptors (GPCRS) signaling and trafficking. Following stimulation, activated receptors are phosphorylated, thus allowing the binding of arrestins and hence an “arrest” of receptor signaling. Arrestins act by uncoupling receptors from G proteins and contribute to the recruitment of endocytic proteins, such as clathrin, to direct receptor trafficking into the endocytic pathway. Arrestins also serve as adaptor proteins by promoting the recruitment of ubiquitin ligases and participate in the agonist-induced ubiquitylation of receptors, known to have impact on their subcellular localization and stability. Recently, the arrestin family has expanded following the discovery of arrestin-related proteins in other eukaryotes such as yeasts or fungi. Surprisingly, most of these proteins are also involved in the ubiquitylation and endocytosis of plasma membrane proteins, thus suggesting that the role of arrestins as ubiquitin ligase adaptors is at the core of these proteins' functions. Importantly, arrestins are themselves ubiquitylated, and this modification is crucial for their function. In this paper, we discuss recent data on the intricate connections between arrestins and the ubiquitin pathway in the control of endocytosis.http://dx.doi.org/10.1155/2012/242764 |
| spellingShingle | Michel Becuwe Antonio Herrador Rosine Haguenauer-Tsapis Olivier Vincent Sébastien Léon Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family Biochemistry Research International |
| title | Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family |
| title_full | Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family |
| title_fullStr | Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family |
| title_full_unstemmed | Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family |
| title_short | Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family |
| title_sort | ubiquitin mediated regulation of endocytosis by proteins of the arrestin family |
| url | http://dx.doi.org/10.1155/2012/242764 |
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