Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins.

@article{Irobi2004StructuralBO,
  title={Structural basis of actin sequestration by thymosin-beta4: implications for WH2 proteins.},
  author={Edward Irobi and Adeleke Halilu Aguda and M{\aa}rten Larsson and Christophe Gu{\'e}rin and Helen L. Yin and Leslie D. Burtnick and Laurent Blanchoin and Robert C Robinson},
  journal={The EMBO journal},
  year={2004},
  volume={23 18},
  pages={3599-608}
}
The WH2 (Wiscott-Aldridge syndrome protein homology domain 2) repeat is an actin interacting motif found in monomer sequestering and filament assembly proteins. We have stabilized the prototypical WH2 family member, thymosin-beta4 (Tbeta4), with respect to actin, by creating a hybrid between gelsolin domain 1 and the C-terminal half of Tbeta4 (G1-Tbeta4). This hybrid protein sequesters actin monomers, severs actin filaments and acts as a leaky barbed end cap. Here, we present the structure of… CONTINUE READING

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The b - thymosin / WH 2 domain : structural basis for the switch from inhibition to promotion of actin assembly

  • M Hertzog, EG Yarmola, D Didry, MR Bubb, MF Carlier
  • Cell
  • 2004
Highly Influential
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