Title |
A Novel Rab5 GDP/GTP Exchange Factor Complexed to Rabaptin-5 Links Nucleotide Exchange to Effector Recruitment and Function
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Published in |
Cell, September 1997
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DOI | 10.1016/s0092-8674(00)80380-3 |
Pubmed ID | |
Authors |
Hisanori Horiuchi, Roger Lippé, Heidi M. McBride, Mariantonietta Rubino, Philip Woodman, Harald Stenmark, Vladimir Rybin, Matthias Wilm, Keith Ashman, Matthias Mann, Marino Zerial |
Abstract |
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 striking homology to Vps9p, a yeast protein implicated in endocytic traffic. Rabex-5 displays GDP/GTP exchange activity on Rab5 upon delivery of the GTPase to the membrane. This demonstrates that a soluble exchange factor coupled to a Rab effector translocates from cytosol to the membrane, where the complex stabilizes the GTPase in the active state. |
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Geographical breakdown
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United States | 4 | 2% |
United Kingdom | 3 | 1% |
Hungary | 2 | <1% |
Canada | 1 | <1% |
India | 1 | <1% |
Unknown | 198 | 93% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 38 | 18% |
Student > Master | 19 | 9% |
Professor | 15 | 7% |
Student > Bachelor | 14 | 7% |
Other | 40 | 19% |
Unknown | 27 | 13% |
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Immunology and Microbiology | 4 | 2% |
Other | 12 | 6% |
Unknown | 30 | 14% |