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A Global Protein Kinase and Phosphatase Interaction Network in Yeast

2010; American Association for the Advancement of Science; Volume: 328; Issue: 5981 Linguagem: Inglês

10.1126/science.1176495

1095-9203

Ashton Breitkreutz, Hyungwon Choi, Jeffrey R. Sharom, Lorrie Boucher, Victor Neduva, Brett Larsen, Zhen-Yuan Lin, Bobby-Joe Breitkreutz, Chris Stark, Guomin Liu, Jessica Ahn, Danielle Dewar‐Darch, Teresa Reguly, Xiaojing Tang, Ricardo Almeida, Zhaohui Qin, Tony Pawson, Anne‐Claude Gingras, Alexey I. Nesvizhskii, Mike Tyers,

Cellular transport and secretion

Budding Yeast Kinome Revealed Covalent modification of proteins by phosphorylation is a primary means by which cells control the biochemical activities and functions of proteins. To better understand the full spectrum of cellular control mechanisms mediated by phosphorylation, Breitkreutz et al. (p. 1043 ; see the Perspective by Levy et al. ) used mass spectrometry to identify proteins that interacted with the complete set of protein kinases from budding yeast and with other molecules, including phosphatases, which influence phosphorylation reactions. The results reveal a network of interacting protein kinases and phosphatases, and analysis of other interacting proteins suggests previously undiscovered roles for many of these enzymes.