Global analysis of protein phosphorylation in yeast

Jason Ptacek, Geeta Devgan, Gregory Michaud, Heng Zhu, Xiaowei Zhu, Joseph Fasolo, Hong Guo, Ghil Jona, Ashton Breitkreutz, Richelle Sopko, Rhonda R. McCartney, Martin C. Schmidt, Najma Rachidi, Soo-Jung Lee, Angie S. Mah, Lihao Meng, Michael J. R. Stark, David F. Stern, Claudio De Virgilio, Mike Tyers, Brenda Andrews, Mark Gerstein, Barry Schweitzer, Paul F. Predki and Michael Snyder ()
Additional contact information
Jason Ptacek: Department of Molecular Biophysics and Biochemistry
Geeta Devgan: Yale University
Gregory Michaud: Invitrogen Corporation
Heng Zhu: Yale University
Xiaowei Zhu: Yale University
Joseph Fasolo: Yale University
Hong Guo: Invitrogen Corporation
Ghil Jona: Yale University
Ashton Breitkreutz: University of Toronto, 1 King's College Circle
Richelle Sopko: University of Toronto, 1 King's College Circle
Rhonda R. McCartney: University of Pittsburgh School of Medicine
Martin C. Schmidt: University of Pittsburgh School of Medicine
Najma Rachidi: School of Life Sciences, University of Dundee
Soo-Jung Lee: Yale University School of Medicine
Angie S. Mah: California Institute of Technology
Lihao Meng: Invitrogen Corporation
Michael J. R. Stark: School of Life Sciences, University of Dundee
David F. Stern: Yale University School of Medicine
Claudio De Virgilio: University of Geneva
Mike Tyers: University of Toronto, 1 King's College Circle
Brenda Andrews: University of Toronto, 1 King's College Circle
Mark Gerstein: Department of Molecular Biophysics and Biochemistry
Barry Schweitzer: Invitrogen Corporation
Paul F. Predki: Invitrogen Corporation
Michael Snyder: Department of Molecular Biophysics and Biochemistry

Nature, 2005, vol. 438, issue 7068, 679-684

Abstract: Kinases on the map Protein phosphorylation is involved in the regulation of many basic cellular processes, so it is a prime target for analysis by proteomics. Proteome chip technology has now been used to produce a first-generation map of the global phosphorylation networks in yeast. More than 4,000 interactions were found for over 1,300 proteins, and substrates were identified for the majority of yeast kinases. Many of the yeast proteins and pathways are conserved in other eukaryotes, so this new resource will be of relevance to the mechanisms of protein phosphorylation in many other organisms. All of the data are freely available in a searchable format.

Date: 2005
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DOI: 10.1038/nature04187

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