A Novel Rab5 GDP/GTP Exchange Factor Complexed to Rabaptin-5 Links Nucleotide Exchange to Effector Recruitment and Function

@article{Horiuchi1997ANR,
  title={A Novel Rab5 GDP/GTP Exchange Factor Complexed to Rabaptin-5 Links Nucleotide Exchange to Effector Recruitment and Function},
  author={Hisanori Horiuchi and Roger Lipp{\'e} and Heidi M McBride and Mariantonietta Rubino and Philip Woodman and Harald Stenmark and Vladimir Rybin and Matthias Wilm and Keith Ashman and Matthias Mann and Marino Zerial},
  journal={Cell},
  year={1997},
  volume={90},
  pages={1149-1159}
}
The small GTPase Rab5 plays an essential role in endocytic traffic. Rab GDP dissociation inhibitor delivers Rab5 to the membrane, where a nucleotide exchange activity allows recruitment of an effector protein, Rabaptin-5. Here we uncovered a novel 60 kDa Rab5-binding protein, Rabex-5. Rabex-5 forms a tight physical complex with Rabaptin-5, and this complex is essential for endocytic membrane fusion. Sequencing of mammalian Rabex-5 by nanoelectrospray mass spectrometry and cloning revealed… CONTINUE READING
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