Two distinct effectors of the small GTPase Rab5 cooperate in endocytic membrane fusion.

@article{Gournier1998TwoDE,
  title={Two distinct effectors of the small GTPase Rab5 cooperate in endocytic membrane fusion.},
  author={H{\'e}l{\`e}na Gournier and Harald Stenmark and Vladimir Rybin and Roger Lipp{\'e} and Marino Zerial},
  journal={The EMBO journal},
  year={1998},
  volume={17 7},
  pages={1930-40}
}
Using the yeast two-hybrid system, we have identified a novel 62 kDa coiled-coil protein that specifically interacts with the GTP-bound form of Rab5, a small GTPase that regulates membrane traffic in the early endocytic pathway. This protein shares 42% sequence identity with Rabaptin-5, a previously identified effector of Rab5, and we therefore named it Rabaptin-5beta. Like Rabaptin-5, Rabaptin-5beta displays heptad repeats characteristic of coiled-coil proteins and is recruited on the… CONTINUE READING

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