Regulation of dynamin oligomerization in cells: the role of dynamin-actin interactions and its GTPase activity.

@article{Gu2014RegulationOD,
  title={Regulation of dynamin oligomerization in cells: the role of dynamin-actin interactions and its GTPase activity.},
  author={Changkyu Gu and Joann Y. Chang and Valentina A Shchedrina and Vincent A Pham and John H. Hartwig and Worawit Suphamungmee and William Lehman and Bradley T. Hyman and Brian J. Bacskai and S. JantraS B. B. Alvarez D. M. Sever},
  journal={Traffic},
  year={2014},
  volume={15 8},
  pages={819-38}
}
Dynamin is a 96-kDa protein that has multiple oligomerization states that influence its GTPase activity. A number of different dynamin effectors, including lipids, actin filaments, and SH3-domain-containing proteins, have been implicated in the regulation of dynamin oligomerization, though their roles in influencing dynamin oligomerization have been studied predominantly in vitro using recombinant proteins. Here, we identify higher order dynamin oligomers such as rings and helices in vitro and… CONTINUE READING
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