The small GTPase RalA targets filamin to induce filopodia
AUTOR(ES)
Ohta, Yasutaka
FONTE
The National Academy of Sciences
RESUMO
The Ras-related small GTPases Rac, Rho, Cdc42, and RalA bind filamin, an actin filament-crosslinking protein that also links membrane and other intracellular proteins to actin. Of these GTPases only RalA binds filamin in a GTP-specific manner, and GTP-RalA elicits actin-rich filopods on surfaces of Swiss 3T3 cells and recruits filamin into the filopodial cytoskeleton. Either a dominant negative RalA construct or the RalA-binding domain of filamin 1 specifically block Cdc42-induced filopod formation, but a Cdc42 inhibitor does not impair RalA’s effects, which, unlike Cdc42, are Rac independent. RalA does not generate filopodia in filamin-deficient human melanoma cells, whereas transfection of filamin 1 restores the functional response. RalA therefore is a downstream intermediate in Cdc42-mediated filopod production and uses filamin in this pathway.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=26747Documentos Relacionados
- Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase
- Coding sequences of human ralA and ralB cDNAs.
- RalA but Not RalB Enhances Polarized Delivery of Membrane Proteins to the Basolateral Surface of Epithelial Cells
- Activation of the Small GTPase Ral in Platelets
- Functional association between Arf and RalA in active phospholipase D complex
