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- Title
Endocytic protein intersectin-l regulates actin assembly via Cdc42 and N-WASP.
- Authors
Hussain, N K; Jenna, S; Glogauer, M; Quinn, C C; Wasiak, S; Guipponi, M; Antonarakis, S E; Kay, B K; Stossel, T P; Lamarche-Vane, N; McPherson, P S
- Abstract
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.
- Publication
Nature cell biology, 2001, Vol 3, Issue 10, p927
- ISSN
1465-7392
- Publication type
Journal Article
- DOI
10.1038/ncb1001-927