Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP.

Intersectin-s is a modular scaffolding protein regulating the formation of clathrin-coated vesicles. In addition to the Eps15 homology (EH) and Src homology 3 (SH3) domains of intersectin-s, the neuronal variant (intersectin-l) also has Dbl homology (DH), pleckstrin homology (PH) and C2 domains. We now show that intersectin-l functions through its ...
DH domain as a guanine nucleotide exchange factor (GEF) for Cdc42. In cultured cells, expression of DH-domain-containing constructs cause actin rearrangements specific for Cdc42 activation. Moreover, in vivo studies reveal that stimulation of Cdc42 by intersectin-l accelerates actin assembly via N-WASP and the Arp2/3 complex. N-WASP binds directly to intersectin-l and upregulates its GEF activity, thereby generating GTP-bound Cdc42, a critical activator of N-WASP. These studies reveal a role for intersectin-l in a novel mechanism of N-WASP activation and in regulation of the actin cytoskeleton.
Mesh Terms:
Actins, Adaptor Proteins, Vesicular Transport, Animals, Carrier Proteins, Cell Line, Genes, Reporter, Humans, Microscopy, Confocal, Models, Biological, Nerve Tissue Proteins, Neutrophils, Phalloidine, Protein Structure, Tertiary, Recombinant Fusion Proteins, Wiskott-Aldrich Syndrome Protein, Neuronal, cdc42 GTP-Binding Protein
Nat. Cell Biol.
Date: Oct. 01, 2001
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