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Roles of GRK2 in Cell Signaling Beyond GPCR Desensitization: GRK2-HDAC6 Interaction Modulates Cell Spreading and Motility

AutorPenela, Petronila ; Lafarga, Vanesa ; Tapia, Olga; Rivas, Verónica ; Nogués, Laura ; Lucas, Elisa ; Vila-Bedmar, Rocío ; Murga, Cristina ; Mayor Menéndez, Federico
Fecha de publicación2012
EditorAmerican Association for the Advancement of Science
CitaciónScience Signaling 5 (224) pt 3: 1-4 (2012)
ResumenG protein–coupled receptor kinase 2 (GR K2) is a ubiquitous, essential protein kinase that is emerging as an integrative node in many signaling networks. Moreover, changes in GR K2 abundance and activity have been identified in several inflammatory, cardiovascular disease, and tumor contexts, suggesting that those alterations may contribute to the initiation or development of pathologies. GR Ks were initially identified as key players in the desensitization and internalization of multiple G protein– coupled receptors (GPCR s), but GR K2 also phosphorylates several non-GPCR substrates and dynamically associates with a variety of proteins related to signal transduction. Ongoing research in our laboratory is aimed at understanding how specific GR K2 interactomes are orchestrated in a stimulus-, context-, or cell type– specific manner. We have recently identified an interaction between GR K2 and histone deacetylase 6 (HDAC 6) that modulates cell spreading and motility. HDAC 6 is a major cytoplasmic a-tubulin deacetylase that is involved in cell motility and adhesion. GR K2 dynamically and directly associates with and phosphorylates HDAC 6 to stimulate its a-tubulin deacetylase activity at specific cellular localizations, such as the leading edge of migrating cells, thus promoting local tubulin deacetylation and enhanced motility. GR K2-HDAC 6–mediated regulation of tubulin acetylation also modulates cellular spreading. This GR K2-HDAC 6 functional interaction may have important implications in pathological contexts related to epithelial cell migration
Identificadoresdoi: 10.1126/scisignal.2003098
issn: 1937-9145
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