Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.

@article{Itzen2006NucleotideEV,
  title={Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.},
  author={Aymelt Itzen and Olena Pylypenko and Roger S. Goody and Kirill Alexandrov and Alexey V Rak},
  journal={The EMBO journal},
  year={2006},
  volume={25 7},
  pages={1445-55}
}
Rab GTPases function as essential regulators of vesicle transport in eukaryotic cells. MSS4 was shown to stimulate nucleotide exchange on Rab proteins associated with the exocytic pathway and to have nucleotide-free-Rab chaperone activity. A detailed kinetic analysis of MSS4 interaction with Rab8 showed that MSS4 is a relatively slow exchange factor that forms a long-lived nucleotide-free complex with RabGTPase. In contrast to other characterized exchange factor-GTPase complexes, MSS4:Rab8… CONTINUE READING