Publication: Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin
Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin
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Penengo, L., Mapelli, M., Murachelli, A. G., Confalonieri, S., Magri, L., Musacchio, A., Di Fiore, P. P., Polo, S., & Schneider, T. R. (2006). Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. Cell, 124, 1183–1195. https://doi.org/10.1016/j.cell.2006.02.020
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The interaction between ubiquitinated proteins and intracellular proteins harboring ubiquitin binding domains (UBDs) is critical to a multitude of cellular processes. Here, we report that Rabex-5, a guanine nucleotide exchange factor for Rab5, binds to Ub through two independent UBDs. These UBDs determine a number of properties of Rabex-5, including its coupled monoubiquitination and interaction in vivo with ubiquitinated EGFRs. Structural and biochemical characterization of the UBDs of Rabex-5 revealed that one of them (MIU, motif in
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- Penengo, Lorenza
- Mapelli, Marina
- Murachelli, Andrea G
- Confalonieri, Stefano
- Magri, Laura
- Musacchio, Andrea
- Di Fiore, Pier Paolo
- Polo, Simona
- Schneider, Thomas R
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Penengo, L., Mapelli, M., Murachelli, A. G., Confalonieri, S., Magri, L., Musacchio, A., Di Fiore, P. P., Polo, S., & Schneider, T. R. (2006). Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. Cell, 124, 1183–1195. https://doi.org/10.1016/j.cell.2006.02.020
