title: K11-linked ubiquitin chains as novel regulators of cell division.
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.
authors: Department of Molecular and Cell Biology, University of California at Berkeley, Berkeley, USA.
authors: Katherine E
authors: KE
authors: Wickliffe
authors: Adam
authors: A
authors: Williamson
authors: Hermann-Josef
authors: HJ
authors: Meyer
authors: Aileen
authors: A
authors: Kelly
authors: Michael
authors: M
authors: Rape
mesh_terms: D064173:Anaphase-Promoting Complex-Cyclosome; D000818:Animals; D002455:Cell Division; D006801:Humans; D025821:Polyubiquitin / Q000502:physiology*; D055503:Protein Multimerization; D043743:Ubiquitin-Protein Ligase Complexes / Q000378:metabolism; D057149:Ubiquitinated Proteins / Q000378:metabolism; D054875:Ubiquitination
chemical_list: D057149:Ubiquitinated Proteins; D025821:Polyubiquitin; D043743:Ubiquitin-Protein Ligase Complexes; D064173:Anaphase-Promoting Complex-Cyclosome