Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53.

@article{Millard2005StructuralBO,
  title={Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53.},
  author={Thomas H. Millard and Guillaume Bompard and Man Yeung Heung and Timothy R. Dafforn and David J. Scott and Laura M Machesky and Klaus F{\"u}tterer},
  journal={The EMBO journal},
  year={2005},
  volume={24 2},
  pages={
          240-50
        }
}
The scaffolding protein insulin receptor tyrosine kinase substrate p53 (IRSp53), a ubiquitous regulator of the actin cytoskeleton, mediates filopodia formation under the control of Rho-family GTPases. IRSp53 comprises a central SH3 domain, which binds to proline-rich regions of a wide range of actin regulators, and a conserved N-terminal IRSp53/MIM homology domain (IMD) that harbours F-actin-bundling activity. Here, we present the crystal structure of this novel actin-bundling domain revealing… CONTINUE READING
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