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The chromosome passenger complex (CPC) controls chromosome congression, kinetochore-microtubule attachments, and spindle checkpoint signaling during mitosis. Aurora-B kinase is the catalytic subunit of the CPC. To understand how a single kinase can regulate such diverse events, we have investigated the activation of Aurora-B and describe two distinct activation mechanisms. First, Aurora-B activation in vitro requires two cofactors, telophase disc-60kD (TD-60) and microtubules. TD-60 is critical to localize both the CPC and Haspin kinase activity to centromeres and thus regulates Aurora-B at several levels. Second, Aurora-B substrates can inhibit kinase activation, and this is relieved by phosphorylation of these substrates by the centromeric kinases Plk1 and Haspin. These regulatory mechanisms suggest models for phosphorylation by Aurora-B of centromeric substrates at unaligned chromosomes and merotelic attachments.

Original publication

DOI

10.1126/science.1148980

Type

Journal article

Journal

Science (New York, N.Y.)

Publication Date

01/2008

Volume

319

Pages

469 - 472

Addresses

Department of Biochemistry and Molecular Genetics, University of Virginia Medical School, Charlottesville, VA 22908, USA.

Keywords

Centromere, Microtubules, Animals, Xenopus, Kinesin, Protein-Serine-Threonine Kinases, Intracellular Signaling Peptides and Proteins, Xenopus Proteins, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, Histones, Mitosis, Enzyme Activation, Phosphorylation, Aurora Kinases