β-Arrestins regulate a Ral-GDS–Ral effector pathway that mediates cytoskeletal reorganization
- 8 July 2002
- journal article
- Published by Springer Nature in Nature Cell Biology
- Vol. 4 (8) , 547-555
- https://doi.org/10.1038/ncb821
Abstract
Beta-Arrestins are important in chemoattractant receptor-induced granule release, a process that may involve Ral-dependent regulation of the actin cytoskeleton. We have identified the Ral GDP dissociation stimulator (Ral-GDS) as a beta-arrestin-binding protein by yeast two-hybrid screening and co-immunoprecipitation from human polymorphonuclear neutrophilic leukocytes (PMNs). Under basal conditions, Ral-GDS is localized to the cytosol and remains inactive in a complex formed with beta-arrestins. In response to formyl-Met-Leu-Phe (fMLP) receptor stimulation, beta-arrestin Ral-GDS protein complexes dissociate and Ral-GDS translocates with beta-arrestin from the cytosol to the plasma membrane, resulting in the Ras-independent activation of the Ral effector pathway required for cytoskeletal rearrangement. The subsequent re-association of beta-arrestin Ral-GDS complexes is associated with the inactivation of Ral signalling. Thus, beta-arrestins regulate multiple steps in the Ral-dependent processes that result in chemoattractant-induced cytoskeletal reorganization.Keywords
This publication has 42 references indexed in Scilit:
- Rab5 Association with the Angiotensin II Type 1A Receptor Promotes Rab5 GTP Binding and Vesicular FusionJournal of Biological Chemistry, 2002
- β-Arrestin-mediated ADP-ribosylation Factor 6 Activation and β2-Adrenergic Receptor EndocytosisJournal of Biological Chemistry, 2001
- The Brain Exocyst Complex Interacts with RalA in a GTP-dependent MannerPublished by Elsevier ,2001
- Small GTP-Binding Protein Ral Modulates Regulated Exocytosis of von Willebrand Factor by Endothelial CellsArteriosclerosis, Thrombosis, and Vascular Biology, 2001
- β-Arrestin1 Interacts with the Catalytic Domain of the Tyrosine Kinase c-SRCJournal of Biological Chemistry, 2000
- N-Formylpeptides Induce Two Distinct Concentration Optima for Mouse Neutrophil Chemotaxis by Differential Interaction with Two N-Formylpeptide Receptor (Fpr) SubtypesThe Journal of Experimental Medicine, 1999
- Ral and Rho-Dependent Activation of Phospholipase D in v-Raf-Transformed CellsBiochemical and Biophysical Research Communications, 1999
- Plasma membrane recruitment of RalGDS is critical for Ras-dependent Ral activationOncogene, 1999
- Cell Migration: A Physically Integrated Molecular ProcessPublished by Elsevier ,1996
- Association of three small GTP‐binding proteins with cholinergic synaptic vesiclesFEBS Letters, 1993