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          Document History for Document ID 585128

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Document Version Version Comment Date Status
585128.0 Automatic journal name synchronization 19.03.2012 17:02 Released

ID: 585128.0, MPI für molekulare Zellbiologie und Genetik / Publikationen MPI-CBG 2011-arch
Systematic phosphorylation analysis of human mitotic protein complexes.
Authors:Hegemann, Björn; Hutchins, James R A; Hudecz, Otto; Novatchkova, Maria; Rameseder, Jonathan; Sykora, Martina M; Liu, Shang-Yun; Mazanek, Michael; Lénárt, Péter; Hériché, Jean-Karim; Poser, Ina; Kraut, Norbert; Hyman, Anthony A.; Yaffe, Michael B; Mechtler, Karl; Peters, Jan-Michael
Date of Publication (YYYY-MM-DD):2011
Title of Journal:Science Signaling
Volume:4
Issue / Number:198
Sequence Number of Article:rs12
Copyright:not available
Review Status:not specified
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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.
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:thuem
Affiliations:MPI für molekulare Zellbiologie und Genetik
Identifiers:LOCALID:4615