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. (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.
A. Breitkreutz, H. Choi, J. R. Sharom, L. Boucher, V. Neduva, B. Larsen, Z.-Y. Lin, B.-J. Breitkreutz, C. Stark, G. Liu, J. Ahn, D. Dewar-Darch, T. Reguly, X. Tang, R. Almeida, Z. S. Qin, T. Pawson, A.-C. Gingras, A. I. Nesvizhskii, M. Tyers, A global protein kinase and phosphatase interaction network in yeast. Science 328, 1043–1046 (2010). [Abstract] [Full Text]