Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization.

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.
Mesh Terms:
Animals, Arrestins, Biological Transport, Active, COS Cells, Cell Line, Cell Membrane, Cytoskeleton, Guanosine 5'-O-(3-Thiotriphosphate), Humans, Macromolecular Substances, Models, Biological, N-Formylmethionine Leucyl-Phenylalanine, Neutrophils, Rats, Receptors, Formyl Peptide, Receptors, Immunologic, Receptors, Peptide, Signal Transduction, Two-Hybrid System Techniques, ral GTP-Binding Proteins, ral Guanine Nucleotide Exchange Factor
Nat. Cell Biol.
Date: Aug. 01, 2002
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