Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes 
of interaction with ubiquitin

Penengo, Lorenza; Mapelli, Marina; Murachelli, Andrea G.; Confalonieri, Stefano; Magri, Laura; Musacchio, Andrea; Di Fiore, Pier Paolo; Polo, Simona; Schneider, Thomas R.

doi:10.1016/j.cell.2006.02.020

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Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin

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Musacchio, Andrea
Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Penengo, L., Mapelli, M., Murachelli, A. G., Confalonieri, S., Magri, L., Musacchio, A., et al. (2006). Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin. CELL, 124(6), 1183-1195. doi:10.1016/j.cell.2006.02.020.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-3B06-A

Abstract

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 interacting with ubiquitin) binds to Ub with modes superimposable to those of the UIM (ubiquitin-interacting motif):Ub interaction, although in the opposite orientation, The other UBD, RUZ (Rabex-5 ubiquitin binding zinc finger) binds to a surface of Ub centered on Asp58(Ub) and distinct from the "canonical" Ile44(Ub)-based surface. The two binding surfaces allow Ub to interact simultaneously with different UBDs, thus opening new perspectives in Ub-mediated signaling.