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Sci. Signal., 29 January 2008
Vol. 1, Issue 4, p. ec32
[DOI: 10.1126/stke.14ec32]

EDITORS' CHOICE

Cell Biology Activating Aurora

Guy Riddihough

Science, AAAS, Washington, DC 20005, USA

Cell division in eukaryotes requires tight spatial and temporal control of its many components. Aurora B kinase, as part of the chromosomal passenger complex (CPC), plays a critical role in regulating chromosome segregation to daughter cells. How is the activity of Aurora B itself controlled? Rosasco-Nitcher et al. show that Aurora B is regulated at several levels by the protein teleophase disc 60-kD (TD-60), which, like Aurora B, is also found at inner centromeres during metaphase. Interaction with TD-60 brings the CPC to the centromere and, in combination with microtubules, activates Aurora B. Furthermore, Aurora B can only act on previously phosphorylated substrates, whose phosphorylation is also enhanced by TD-60. Thus, TD-60 may function to ensure that high levels of Aurora B activity occur only at centromeres.

S. E. Rosasco-Nitcher, W. Lan, S. Khorasanizadeh, P. T. Stukenberg, Centromeric Aurora-B activation requires TD-60, microtubules, and substrate priming phosphorylation. Science 319, 469-472 (2008). [Abstract] [Full Text]

Citation: G. Riddihough, Activating Aurora. Sci. Signal. 1, ec32 (2008).


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