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Sci. Signal., 28 June 2011
Vol. 4, Issue 179, p. rs5
Building the Corpus of Substrates of Mitotic Kinases
Mitosis is a complex process involving duplication of DNA, nuclear membrane dissolution, construction of a mitotic spindle, proper segregation of chromosomes, and, finally, creation of two new cells—each with a complete set of genomic material. Protein phosphorylation plays a critical role in this process and is mediated predominantly by three sets of kinases: the cyclin-dependent kinase–cyclin complex Cdk1/cyclinB, the Aurora family (Aurora A and B), and the Polo-like kinase (Plk) family, especially Plk1. To explore the targets of these kinases, Kettenbach et al. combined specific small-molecule kinase inhibitors with large-scale quantitative phosphoproteomics of mitotic mammalian cells. Their data enable refinement of the motifs recognized by these kinases and suggest previously unknown functions for these kinases, as well as serve as a useful resource for future exploration of these essential mitotic regulators.
Citation: A. N. Kettenbach, D. K. Schweppe, B. K. Faherty, D. Pechenick, A. A. Pletnev, S. A. Gerber, Quantitative Phosphoproteomics Identifies Substrates and Functional Modules of Aurora and Polo-Like Kinase Activities in Mitotic Cells. Sci. Signal.4, rs5 (2011).
Stella M. Hurtley (5 March 2013) Sci. Signal.6 (265), ec59.
[DOI: 10.1126/scisignal.2004115] |Abstract »
Stella M. Hurtley (17 April 2012) Sci. Signal.5 (220), ec115.
[DOI: 10.1126/scisignal.2003136] |Abstract »
Björn Hegemann, James R. A. Hutchins, Otto Hudecz, Maria Novatchkova, Jonathan Rameseder, Martina M. Sykora, Sihan Liu, Michael Mazanek, Péter Lénárt, Jean-Karim Hériché, Ina Poser, Norbert Kraut, Anthony A. Hyman, Michael B. Yaffe, Karl Mechtler, and Jan-Michael Peters (8 November 2011) Sci. Signal.4 (198), rs12.
[DOI: 10.1126/scisignal.2001993] |Editor's Summary »|Abstract »|Full Text »|PDF »|Supplementary Materials »
Jes Alexander, Daniel Lim, Brian A. Joughin, Björn Hegemann, James R. A. Hutchins, Tobias Ehrenberger, Frank Ivins, Fabio Sessa, Otto Hudecz, Erich A. Nigg, Andrew M. Fry, Andrea Musacchio, P. Todd Stukenberg, Karl Mechtler, Jan-Michael Peters, Stephen J. Smerdon, and Michael B. Yaffe (28 June 2011) Sci. Signal.4 (179), ra42.
[DOI: 10.1126/scisignal.2001796] |Editor's Summary »|Abstract »|Full Text »|PDF »|Supplementary Materials »
Jesper V. Olsen, Michiel Vermeulen, Anna Santamaria, Chanchal Kumar, Martin L. Miller, Lars J. Jensen, Florian Gnad, Jürgen Cox, Thomas S. Jensen, Erich A. Nigg, Søren Brunak, and Matthias Mann (12 January 2010) Sci. Signal.3 (104), ra3.
[DOI: 10.1126/scisignal.2000475] |Editor's Summary »|Abstract »|Full Text »|PDF »|Supplementary Materials »
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Identification of Direct Tyrosine Kinase Substrates Based on Protein Kinase Assay-Linked Phosphoproteomics.
Cdk1 and Plk1 mediate a CLASP2 phospho-switch that stabilizes kinetochore-microtubule attachments.
A. R. R. Maia, Z. Garcia, L. Kabeche, M. Barisic, S. Maffini, S. Macedo-Ribeiro, I. M. Cheeseman, D. A. Compton, I. Kaverina, and H. Maiato (2012)
J. Cell Biol.
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Plk1 Phosphorylates Sgt1 at the Kinetochores To Promote Timely Kinetochore-Microtubule Attachment.