A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex

@article{Panchal2003ACA,
  title={A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex},
  author={Sanjay C. Panchal and Donald A. Kaiser and Eduardo R. Torres and Thomas D. Pollard and Michael K Rosen},
  journal={Nature Structural Biology},
  year={2003},
  volume={10},
  pages={591-598}
}
Members of the Wiskott-Aldrich syndrome protein (WASP) family link Rho GTPase signaling pathways to the cytoskeleton through a multiprotein assembly called Arp2/3 complex. The C-terminal VCA regions (verprolin-homology, central hydrophobic, and acidic regions) of WASP and its relatives stimulate Arp2/3 complex to nucleate actin filament branches. Here we show by differential line broadening in NMR spectra that the C (central) and A (acidic) segments of VCA domains from WASP, N-WASP and Scar… CONTINUE READING

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