Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis

@article{Sever1999ImpairmentOD,
  title={Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis},
  author={S. JantraS B. B. Alvarez D. M. Sever and Amy B. Muhlberg and Sandra L Schmid},
  journal={Nature},
  year={1999},
  volume={398},
  pages={481-486}
}
Dynamin is a GTP-hydrolysing protein that is an essential participant in clathrin-mediated endocytosis by cells. It self-assembles into ‘collars’ in vitro which also form in vivo at the necks of invaginated coated pits. This self-assembly stimulates dynamin's GTPase activity and it has been proposed that dynamin hydrolyses GTP in order to generate the force needed to sever vesicles from the plasma membrane. A mechanism is now described in which self-assembly of dynamin is coordinated by a… CONTINUE READING
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