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

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.

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Penengo, Lorenza1, Author
Mapelli, Marina1, Author
Murachelli, Andrea G.1, Author
Confalonieri, Stefano1, Author
Magri, Laura1, Author
Musacchio, Andrea2, Author           
Di Fiore, Pier Paolo1, Author
Polo, Simona1, Author
Schneider, Thomas R.1, Author
Affiliations:
1IFOM, the FIRC Institute for Molecular Oncology Foundation, Via Adamello 16, 20139 Milan, Italy, ou_persistent22              
2Abt. I:Mechanistische Zellbiologie, Max Planck Institute of Molecular Physiology, Max Planck Society, ou_1753287              

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 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.

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 Dates: 2006
 Publication Status: Issued
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Title: CELL
Source Genre: Journal
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Pages: - Volume / Issue: 124 (6) Sequence Number: - Start / End Page: 1183 - 1195 Identifier: ISSN: 0092-8674