Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission

@article{Bielli2005RegulationOS,
  title={Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission},
  author={Anna Bielli and Charles J. Haney and Gavin Gabreski and Simon C. Watkins and Sergei I Bannykh and Meir Aridor},
  journal={The Journal of Cell Biology},
  year={2005},
  volume={171},
  pages={919 - 924}
}
The mechanisms by which the coat complex II (COPII) coat mediates membrane deformation and vesicle fission are unknown. Sar1 is a structural component of the membrane-binding inner layer of COPII (Bi, X., R.A. Corpina, and J. Goldberg. 2002. Nature. 419:271-277). Using model liposomes we found that Sar1 uses GTP-regulated exposure of its NH2-terminal tail, an amphipathic peptide domain, to bind, deform, constrict, and destabilize membranes. Although Sar1 activation leads to constriction of… CONTINUE READING
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