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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.

SUBMITTER: Wickliffe KE

PROVIDER: S-EPMC3205209 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature

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K11-linked ubiquitin chains as novel regulators of cell division.

Wickliffe Katherine E KE Williamson Adam A Meyer Hermann-Josef HJ Kelly Aileen A Rape Michael M

Trends in cell biology 20111004 11

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 ...[more]

PMID: 21978762

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