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- W2133059094 abstract "Rabex-5 and Rabaptin-5 function together to activate Rab5 and further promote early endosomal fusion in endocytosis. The Rabex-5 GEF activity is autoinhibited by the Rabex-5 CC domain (Rabex-5CC) and activated by the Rabaptin-5 C2-1 domain (Rabaptin-5C21) with yet unknown mechanism. We report here the crystal structures of Rabex-5 in complex with the dimeric Rabaptin-5C21 (Rabaptin-5C212) and in complex with Rabaptin-5C212 and Rab5, along with biophysical and biochemical analyses. We show that Rabex-5CC assumes an amphipathic α-helix which binds weakly to the substrate-binding site of the GEF domain, leading to weak autoinhibition of the GEF activity. Binding of Rabaptin-5C21 to Rabex-5 displaces Rabex-5CC to yield a largely exposed substrate-binding site, leading to release of the GEF activity. In the ternary complex the substrate-binding site of Rabex-5 is completely exposed to bind and activate Rab5. Our results reveal the molecular mechanism for the regulation of the Rabex-5 GEF activity." @default.
- W2133059094 created "2016-06-24" @default.
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- W2133059094 date "2014-06-23" @default.
- W2133059094 modified "2023-10-10" @default.
- W2133059094 title "Molecular mechanism for Rabex-5 GEF activation by Rabaptin-5" @default.
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- W2133059094 doi "https://doi.org/10.7554/elife.02687" @default.
- W2133059094 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4102244" @default.
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