Autoinhibition and activation mechanisms of the Wiskott–Aldrich syndrome protein

@article{Kim2000AutoinhibitionAA,
  title={Autoinhibition and activation mechanisms of the Wiskott–Aldrich syndrome protein},
  author={Annette S. Kim and Lazaros T. Kakalis and Norzehan Abdul-Manan and Grace A. Liu and Michael K. Rosen},
  journal={Nature},
  year={2000},
  volume={404},
  pages={151-158}
}
The Rho-family GTPase, Cdc42, can regulate the actin cytoskeleton through activation of Wiskott–Aldrich syndrome protein (WASP) family members. Activation relieves an autoinhibitory contact between the GTPase-binding domain and the carboxy-terminal region of WASP proteins. Here we report the autoinhibited structure of the GTPase-binding domain of WASP, which can be induced by the C-terminal region or by organic co-solvents. In the autoinhibited complex, intramolecular interactions with the… 
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  • Biology
    The Journal of Biological Chemistry
  • 2001
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A conserved amphipathic helix in WASP/Scar proteins is essential for activation of Arp2/3 complex
TLDR
It is shown by differential line broadening in NMR spectra that the C (central) and A (acidic) segments of VCA domains from WASP, N-WASP and Scar bind Arp2/3 complex.
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