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. 2001 Oct;3(10):927-32.
doi: 10.1038/ncb1001-927.

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

N K Hussain  1 , S Jenna, M Glogauer, C C Quinn, S Wasiak, M Guipponi, S E Antonarakis, B K Kay, T P Stossel, N Lamarche-Vane, P S McPherson
Affiliations

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

N K Hussain et al. Nat Cell Biol. 2001 Oct.

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.

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