Dimeric endophilin A2 stimulates assembly and GTPase activity of dynamin 2.

@article{Ross2011DimericEA,
  title={Dimeric endophilin A2 stimulates assembly and GTPase activity of dynamin 2.},
  author={Justin Andrew Ross and Yan Chen and Joachim Dipl Ing Mueller and Barbara Barylko and Qian Wang and Hunter B. Banks and Joseph P Albanesi and David Jameson},
  journal={Biophysical journal},
  year={2011},
  volume={100 3},
  pages={
          729-737
        }
}
Endophilin, which participates in membrane vesiculation during receptor-mediated endocytosis, is a ∼40 kDa SH3 domain-containing protein that binds to the proline/arginine-rich domain of dynamin, a ∼100 kDa GTPase that is essential for endocytic membrane scission. It has been suggested that endophilin is monomeric in the cytoplasm and dimerizes only after it binds to membranes (or perhaps to dimers or tetramers of dynamin). To clarify this issue, we studied the oligomeric state of endophilin… CONTINUE READING
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