Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells

Science Signaling

Volumn 4, Issue 179, 2011, Pages

  Kettenbach, Arminja N ^a,b   Schweppe, Devin K ^a   Faherty, Brendan K ^a   Pechenick, Dov ^a   Pletnev, Alexandre A ^b,c   Gerber, Scott A ^a,b  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

^b NORRIS COTTON CANCER CENTER   (United States)

^c Dartmouth College   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

4 (8 CYCLOPENTYL 7 ETHYL 5,6,7,8 TETRAHYDRO 5 METHYL 6 OXO 2 PTERIDINYLAMINO) 3 METHOXY N (1 METHYL 4 PIPERIDINYL)BENZAMIDE; 4 [[9 CHLORO 7 (2,6 DIFLUOROPHENYL) 5H PYRIMIDO[5,4 D][2]BENZAZEPIN 2 YL]AMINO]BENZOIC ACID; AURORA A KINASE; AURORA B KINASE; BARASERTIB; N [4 [6 METHOXY 7 (3 MORPHOLINOPROPOXY) 4 QUINAZOLINYLAMINO]PHENYL]BENZAMIDE; POLO LIKE KINASE; AURORA KINASE; CELL CYCLE PROTEIN; CYCLIN B; CYCLIN DEPENDENT KINASE 1; ONCOPROTEIN; POLO LIKE KINASE 1; POLO-LIKE KINASE 1; PROTEIN SERINE THREONINE KINASE; PROTEOME;

ARTICLE; CELL CYCLE ARREST; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME SUBSTRATE COMPLEX; HUMAN; HUMAN CELL; IN VITRO STUDY; MITOSIS; PEPTIDE MAPPING; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PHOSPHORYLATION; PROTEIN TARGETING; PROTEOMICS; QUANTITATIVE ANALYSIS; SIGNAL TRANSDUCTION; HELA CELL; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN MOTIF;

AMINO ACID MOTIFS; CDC2 PROTEIN KINASE; CELL CYCLE PROTEINS; CYCLIN B; HELA CELLS; HUMANS; MITOSIS; PHOSPHORYLATION; PROTEIN-SERINE-THREONINE KINASES; PROTEOME; PROTEOMICS; PROTO-ONCOGENE PROTEINS; SIGNAL TRANSDUCTION;

EID: 79959735228     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2001497     Document Type: Article

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55. Acknowledgments: We thank D. Compton for providing reagents and for helpful discussions, D. Madden for help with baculovirus protein expression, J. Ruderman for providing active Aurora A kinase, F. McKeon for providing reagents, J. Gilmore and J. Milloy for technical discussions concerning data analysis, S. Cullati for proofreading the manuscript, and Millennium Pharmaceuticals for providing MLN8054. Funding: This work was supported by NIH grant P20-RR018787 from the IDeA Program of the National Center for Research Resources, the American Cancer Society grant IRG-82-003-24 (to S.A.G.), and predoctoral fellowships from the National Institute of General Medical Sciences grant T32-GM008704 (to D.K.S. and B.K.F.). Author contributions: A.N.K. coordinated the project, conducted most of the experimental work, analyzed most of the data, prepared the figures, and drafted the manuscript. D.K.S. conducted the Aurora A inhibitor study. B.K.F. established the informatics pipeline used for quantification and ModSite assignments. D.P. conducted the evolution alignments and data analysis. A.A.P. synthesized BI2536 and AZD1152. S.A.G. conceptualized the study, designed and performed the experiments, analyzed the data, and finalized the manuscript. Competing interests: Compound MLN8054 requires a material transfer agreement (MTA) from Millennium Pharmaceuticals. S.A.G. has a paid consultancy with Millennium Pharmaceuticals relating to the clinical use of MLN8054 as an anticancer agent. Data availability: Raw data files are available through https://proteomecommons.org/ (see Supplementary Materials for codes).