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Updated: May 28, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
Published on: May 14, 2021
K11-linked ubiquitin chains as novel regulators of cell division
Katherine E Wickliffe1, Adam Williamson, Hermann-Josef Meyer
1Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, USA.
Abstract:
Modification of proteins with ubiquitin chains is an essential regulatory event in cell cycle control. Differences in the connectivity of ubiquitin chains are believed to result in distinct functional consequences for the modified proteins. Among eight possible homogenous chain types, canonical Lys48-linked ubiquitin chains have long been recognized to drive the proteasomal degradation of cell cycle regulators, and Lys48 is the only essential lysine residue of ubiquitin in yeast. It thus came as a surprise that in higher eukaryotes atypical K11-linked ubiquitin chains regulate the substrates of the anaphase-promoting complex and control progression through mitosis. We discuss recent findings that shed light on the assembly and function of K11-linked chains during cell division.
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