Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5.

@article{Vitale1998DistinctRD,
  title={Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5.},
  author={Gaetano Vitale and Vladimir Rybin and Savvas Christoforidis and P Thornqvist and Mary McCaffrey and Harald Stenmark and Marino Zerial},
  journal={The EMBO journal},
  year={1998},
  volume={17 7},
  pages={1941-51}
}
Rabaptin-5 functions as an effector for the small GTPase Rab5, a regulator of endocytosis and early endosome fusion. We have searched for structural determinants that confer functional specificity on Rabaptin-5. Here we report that native cytosolic Rabaptin-5 is present in a homodimeric state and dimerization depends upon the presence of its coiled-coil predicted sequences. A 73 residue C-terminal region of Rabaptin-5 is necessary and sufficient both for the interaction with Rab5 and for Rab5… CONTINUE READING
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