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Título: | CXCR4/AckR3 phosphorylation and recruitment of interacting proteins: Key mechanisms regulating their functional status |
Autor: | Fumagalli, Amos; Zarca, Aurélien; Neves, María; Caspar, Birgit; Hill, Stephen J; Mayor Méndez, Federico Jr.; Smith, Martine J.; Marin, Philippe | Fecha de publicación: | 21-feb-2019 | Editor: | American Society for Pharmacology and Experimental Therapeutics | Citación: | Molecular Pharmacology 96: 794- 808 (2019) | Resumen: | The C-X-C motif chemokine receptor type 4 (CXCR4) and the atypical chemokine receptor 3 (ACKR3/CXCR7) are class A G protein-coupled receptors (GPCRs). Accumulating evidence indicates that GPCR subcellular localization, trafficking, transduction properties, and ultimately their pathophysiological functions are regulated by both interacting proteins and post-translational modifications. This has encouraged the development of novel techniques to characterize the GPCR interactome and to identify residues subjected to post-translational modifications, with a special focus on phosphorylation. This review first describes state-of-the-art methods for the identification of GPCR-interacting proteins and GPCR phosphorylated sites. In addition, we provide an overview of the current knowledge of CXCR4 and ACKR3 post-translational modifications and an exhaustive list of previously identified CXCR4- or ACKR3-interacting proteins. We then describe studies highlighting the importance of the reciprocal influence of CXCR4/ACKR3 interactomes and phosphorylation states. We also discuss their impact on the functional status of each receptor. These studies suggest that deeper knowledge of the CXCR4/ACKR3 interactomes along with their phosphorylation and ubiquitination status would shed new light on their regulation and pathophysiological functions. | Versión del editor: | http://dx.doi.org/10.1124/mol.118.115360 | URI: | http://hdl.handle.net/10261/214032 | DOI: | 10.1124/mol.118.115360 | Identificadores: | doi: 10.1124/mol.118.115360 issn: 1521-0111 |
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MayorJrF_CXCR4_ACKR3Phosphorylation.pdf | 567,15 kB | Adobe PDF | Visualizar/Abrir |
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