Cell Reports volume 5, issue 3, P826-838 2013 DOI: 10.1016/j.celrep.2013.10.008 View full text
Miklós Békés, Keiji Okamoto, Sarah B. Crist, Mathew J. Jones, Jessica R. Chapman, Bradley B. Brasher, Francesco D. Melandri, Beatrix M. Ueberheide, Eros Lazzerini Denchi, Tony T. Huang

Abstract: Summary The ubiquitin-modification status of proteins in cells is highly dynamic and maintained by specific ligation machineries (E3 ligases) that tag proteins with ubiquitin or by deubiquitinating enzymes (DUBs) that remove the ubiquitin tag. The development of tools that offset this balance is critical in characterizing signaling pathways that utilize such ubiquitination switches. Herein, we generated a DUB-resistant ubiquitin mutant that is recalcitrant to cleavage by various families of DUBs both in vitro…

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