Comparative analysis reveals conserved protein phosphorylation networks implicated in multiple diseases

Science Signaling

Volumn 2, Issue 81, 2009, Pages

  Tan, Chris Soon Heng ^a,b   Bodenmiller, Bernd ^c   Pasculescu, Adrian ^a   Jovanovic, Marko ^d   Hengartner, Michael O ^d   Claus, Jørgensen ^a   Bader, Gary D ^a,b   Aebersold, Ruedi ^c,d,e   Pawson, Tony ^a,b   Linding, Rune ^f  

^a MOUNT SINAI HOSPITAL   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

^c ETH ZURICH   (Switzerland)

^d UNIVERSITY OF ZURICH   (Switzerland)

^e INSTITUTE FOR SYSTEMS BIOLOGY   (United States)

^f INSTITUTE OF CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOPROTEIN; PROTEOME; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE ACTIVATING KINASE; CYCLIN-DEPENDENT KINASE-ACTIVATING KINASE; PROTEIN;

ARTICLE; CELL FUNCTION; CELL STRUCTURE; CLINICAL FEATURE; COMPARATIVE STUDY; GENE SEQUENCE; GENETIC CONSERVATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PHOSPHORYLATION; SIGNAL TRANSDUCTION; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CAENORHABDITIS ELEGANS; CHEMICAL STRUCTURE; CHEMISTRY; CLASSIFICATION; CLUSTER ANALYSIS; DISEASE PREDISPOSITION; DROSOPHILA MELANOGASTER; GENETICS; HUMAN; METABOLISM; METHODOLOGY; MOLECULAR EVOLUTION; MOLECULAR GENETICS; PATHOPHYSIOLOGY; PHOSPHORYLATION; PHYLOGENY; PHYSIOLOGY; PROTEIN TERTIARY STRUCTURE; PROTEOMICS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CAENORHABDITIS ELEGANS; CLUSTER ANALYSIS; CYCLIN-DEPENDENT KINASES; DISEASE SUSCEPTIBILITY; DROSOPHILA MELANOGASTER; EVOLUTION, MOLECULAR; HUMANS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PHOSPHOPROTEINS; PHOSPHORYLATION; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY; PROTEINS; PROTEOMICS; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; SIGNAL TRANSDUCTION;

EID: 70349526350     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2000316     Document Type: Article

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69. We thank L. J. Jensen (CPR), K. Colwill (SLRI), S. Quirk, and J. Koh for comments on the manuscript. We are further indebted to B. Turk (Yale), S.Michnick (University ofMontreal), P. Beltrao and N. Krogan (University of California, San Francisco) for sharing unpublished results. This project was in part supported by Genome Canada through Ontario Genomics Institute and the Canadian Institutes of Health Research (MOP-84324).We also thank the Functional Genomics Center Zurich for generous support with mass spectrometry resources. This project has been funded in part by ETHZurich, the SwissNational Science Foundation under grant 31000-110767, with Federal (U.S.) funds from the National Heart, Lung, and Blood Institute, NIH, under contract N01-HV-28179, and by theCenter for Model Organism Proteomics of the University of Zurich, the Swiss Initiative for Systems Biology. M.O.H. is the Ernst Hadorn Chair of Molecular Biology. R.A. was supported in part by a grant from F. Hoffmann-LaRoche (Basel) provided to the Competence Center for Systems Physiology andMetabolicDisease. B.B. is the recipient of a fellowship from the Boehringer Ingelheim Fonds. M.J. was supported by a fellowship from the Research Foundation of the University of Zurich and by a fellowship from the Roche Research Foundation. Author contributions: R.L. conceived the project. R.L., C.S.H.T., T.P., R.A., B.B., G.B., and C.J. conceived and designed the experiments. R.L., C.S.H.T., and A.P. performed the computational experiments. B.B. and M.J. performed the proteomics experiments. R.A.,C.S.H.T., B.B., C.J., G.B., T.P., and R.L. wrote the paper.