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The interplay between G protein-coupled receptor kinase 2 (GRK2) and histone deacetylase 6 (HDAC6) at the crossroads of epithelial cell motility

AutorLafarga, Vanesa ; Penela, Petronila ; Mayor Menéndez, Federico
Palabras claveTubulin acetylation
HDAC6
Cell migration
Polarity
Microtubules
GRK2
Fecha de publicación2012
EditorLandes Bioscience
CitaciónCell Adhesion and Migration 6 (6): 495-501 (2012)
ResumenG protein-coupled receptor kinase 2 (GRK2) is emerging as a key integrative node in cell migration control. In addition to its canonical role in the desensitization of G protein-coupled receptors involved in chemotaxis, novel recently identified GRK2 substrates and interacting partners appear to mediate the GRK2-dependent modulation of diverse molecular processes involved in motility, such as gradient sensing, cell polarity or cytoskeletal reorganization. We have recently identified an interaction between GRK2 and histone deacetylase 6 (HDAC6), a major cytoplasmic a -tubulin deacetylase involved in cell motility and adhesion. GRK2 dynamically associates with and phosphorylates HDAC6 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. This GRK2-HDAC6 functional interaction may have important implications in pathological contexts related to aberrant epithelial cell migration.
URIhttp://hdl.handle.net/10261/114816
DOI10.4161/cam.21585
Identificadoresdoi: 10.4161/cam.21585
issn: 1933-6926
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