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  Systematic phosphorylation analysis of human mitotic protein complexes.

Hegemann, B., Hutchins, J. R. A., Hudecz, O., Novatchkova, M., Rameseder, J., Sykora, M. M., et al. (2011). Systematic phosphorylation analysis of human mitotic protein complexes. Science Signaling, 4(198): RS12. doi:10.1126/scisignal.2001993.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0002-0EC6-0 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-0ED0-4
Genre: Journal Article

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 Creators:
Hegemann, B., Author
Hutchins, J. R. A., Author
Hudecz, O., Author
Novatchkova, M., Author
Rameseder, J., Author
Sykora, M. M., Author
Liu, S., Author
Mazanek, M., Author
Lenart, P.1, Author              
Hériché, J. K., Author
Poser, I., Author
Kraut, N., Author
Hyman, A. A., Author
Yaffe, M. B., Author
Mechtler, K., Author
Peters, J. M., Author
Affiliations:
1Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society, ou_2640691              

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 Abstract: Progression through mitosis depends on a large number of protein complexes that regulate the major structural and physiological changes necessary for faithful chromosome segregation. Most, if not all, of the mitotic processes are regulated by a set of mitotic protein kinases that control protein activity by phosphorylation. Although many mitotic phosphorylation events have been identified in proteome-scale mass spectrometry studies, information on how these phosphorylation sites are distributed within mitotic protein complexes and which kinases generate these phosphorylation sites is largely lacking. We used systematic protein-affinity purification combined with mass spectrometry to identify 1818 phosphorylation sites in more than 100 mitotic protein complexes. In many complexes, the phosphorylation sites were concentrated on a few subunits, suggesting that these subunits serve as "switchboards" to relay the kinase-regulatory signals within the complexes. Consequent bioinformatic analyses identified potential kinase-substrate relationships for most of these sites. In a subsequent in-depth analysis of key mitotic regulatory complexes with the Aurora kinase B (AURKB) inhibitor Hesperadin and a new Polo-like kinase (PLK1) inhibitor, BI 4834, we determined the kinase dependency for 172 phosphorylation sites on 41 proteins. Combination of the results of the cellular studies with Scansite motif prediction enabled us to identify 14 sites on six proteins as direct candidate substrates of AURKB or PLK1.

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Language(s): eng - English
 Dates: 2011-11-08
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/scisignal.2001993
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Title: Science Signaling
Source Genre: Journal
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Pages: 17 Volume / Issue: 4 (198) Sequence Number: RS12 Start / End Page: - Identifier: -