A possible effector role for the pleckstrin homology (PH) domain of dynamin.

@article{Bethoney2009APE,
  title={A possible effector role for the pleckstrin homology (PH) domain of dynamin.},
  author={Kelley A. Bethoney and Megan C King and Jenny E. Hinshaw and E Michael Ostap and Mark A Lemmon},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 32},
  pages={13359-64}
}
The large GTPase dynamin plays a key role in clathrin-mediated endocytosis in animal cells, although its mechanism of action remains unclear. Dynamins 1, 2, and 3 contain a pleckstrin homology (PH) domain that binds phosphoinositides with a very low affinity (K(D) > 1 mM), and this interaction appears to be crucial for function. These observations prompted the suggestion that an array of PH domains drives multivalent binding of dynamin oligomers to phosphoinositide-containing membranes… CONTINUE READING

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