The GTPase dynamin binds to and is activated by a subset of SH3 domains.

@article{Gout1993TheGD,
  title={The GTPase dynamin binds to and is activated by a subset of SH3 domains.},
  author={Ivan T. Gout and Ritu Dhand and Ian D Hiles and Michael J. Fry and George N Panayotou and Pamela D Das and Oanh Truong and Nicholas F. Totty and J Justin Hsuan and Grant W Booker},
  journal={Cell},
  year={1993},
  volume={75 1},
  pages={25-36}
}
Src homology 3 (SH3) domains have been implicated in mediating protein-protein interactions in receptor signaling processes; however, the precise role of this domain remains unclear. In this report, affinity purification techniques were used to identify the GTPase dynamin as an SH3 domain-binding protein. Selective binding to a subset of 15 different recombinant SH3 domains occurs through proline-rich sequence motifs similar to those that mediate the interaction of the SH3 domains of Grb2 and… CONTINUE READING
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