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Sci. Signal., 8 November 2011
Vol. 4, Issue 198, p. rs12
[DOI: 10.1126/scisignal.2001993]

RESEARCH RESOURCES

Editor's Summary

Regulating Mitotic Machines
Most proteins do not function in isolation; they are part of large macromolecular complexes. Hegemann et al. used information available about the protein complexes involved in mitosis and then performed mass spectrometry to determine the phosphoproteome of these mitotic machines. Certain proteins in each complex were phosphorylated at many more sites than other proteins in the complex and thus may represent master regulators of the activities of these mitotic machines. Experiments with specific inhibitors of Polo-like kinase 1 and Aurora kinase B enabled the identification of specific targets of these mitotic kinases, providing insight into the mechanism by which these two kinases regulate the activity of mitotic complexes to control progression through the complicated process of cell division.

Citation: B. Hegemann, J. R. A. Hutchins, O. Hudecz, M. Novatchkova, J. Rameseder, M. M. Sykora, S. Liu, M. Mazanek, P. Lénárt, J.-K. Hériché, I. Poser, N. Kraut, A. A. Hyman, M. B. Yaffe, K. Mechtler, J.-M. Peters, Systematic Phosphorylation Analysis of Human Mitotic Protein Complexes. Sci. Signal. 4, rs12 (2011).

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