A dynamin mutant defines a superconstricted prefission state.

@article{Sundborger2014ADM,
  title={A dynamin mutant defines a superconstricted prefission state.},
  author={Anna C. Sundborger and Shunming Fang and Juergen Heymann and Pampa Ray and Joshua S Chappie and Jenny E. Hinshaw},
  journal={Cell reports},
  year={2014},
  volume={8 3},
  pages={734-42}
}
Dynamin is a 100 kDa GTPase that organizes into helical assemblies at the base of nascent clathrin-coated vesicles. Formation of these oligomers stimulates the intrinsic GTPase activity of dynamin, which is necessary for efficient membrane fission during endocytosis. Recent evidence suggests that the transition state of dynamin's GTP hydrolysis reaction serves as a key determinant of productive fission. Here, we present the structure of a transition-state-defective dynamin mutant K44A trapped… CONTINUE READING
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