Conferences
23–28 January 2011, Keystone Resort, Keystone, Colorado, USA
The Evolution of Protein Phosphorylation
Meeting Summary
Major progress has been made in defining the basis of signaling in eukaryotic cells both with respect to the function and structure of protein modules that are involved in signaling and how these proteins are organized into pathways and networks that are used to regulate cellular responses to extracellular and intracellular stimuli. Through intensive studies over the past 40 years protein phosphorylation has become one of the best understood signaling mechanisms. Most of what has been learned has been derived from studies of a few model organisms, which have taught us that several major signal transduction pathways are conserved in evolution. The recent flood of new eukaryotic genome sequences has engendered significant interest in understanding the evolution of the protein kinases and phosphatases and other signaling proteins involved in protein phosphorylation (e.g. where did tyrosine kinases come from?). In addition, the explosion of phosphoproteomic data from multiple organisms (including prokaryotes) indicates that the majority of proteins in the cell may be phosphorylated, leading to questions such as whether all the detected phosphorylation events are functional, and how this can be addressed, especially for highly phosphorylated proteins. Our increasingly systems-based understanding of the genes involved in phosphorylation signaling and the identification of the full spectrum of proteins that are reversibly phosphorylated now makes it possible to ask to what extent phosphorylation of specific sites or regions is conserved during evolution, which may provide important functional insights. In addition to these topics, the meeting would cover the evolution of protein kinases and phosphatases and key signaling modules, such as the SH2 and SH3 domains, and the evolution of protein phosphorylation in prokaryotes and plants and how their systems differ from those in animals. A number of other topics, such as the functional conservation of orthologous proteins involved in phosphorylation, whether phosphorylation network architecture has been conserved, and the evolutionary function of conserved pseudokinases, would be discussed. Clearly for this topic it is particularly important to have as broad a representation as possible from the different areas of protein phosphorylation, we have selected speakers working on a wide range of eukaryotic and prokaryotic organisms in order to emphasize the evolution and conservation of protein phosphorylation.
Major progress has been made in defining the basis of signaling in eukaryotic cells both with respect to the function and structure of protein modules that are involved in signaling and how these proteins are organized into pathways and networks that are used to regulate cellular responses to extracellular and intracellular stimuli. Through intensive studies over the past 40 years protein phosphorylation has become one of the best understood signaling mechanisms. Most of what has been learned has been derived from studies of a few model organisms, which have taught us that several major signal transduction pathways are conserved in evolution. The recent flood of new eukaryotic genome sequences has engendered significant interest in understanding the evolution of the protein kinases and phosphatases and other signaling proteins involved in protein phosphorylation (e.g. where did tyrosine kinases come from?). In addition, the explosion of phosphoproteomic data from multiple organisms (including prokaryotes) indicates that the majority of proteins in the cell may be phosphorylated, leading to questions such as whether all the detected phosphorylation events are functional, and how this can be addressed, especially for highly phosphorylated proteins. Our increasingly systems-based understanding of the genes involved in phosphorylation signaling and the identification of the full spectrum of proteins that are reversibly phosphorylated now makes it possible to ask to what extent phosphorylation of specific sites or regions is conserved during evolution, which may provide important functional insights. In addition to these topics, the meeting would cover the evolution of protein kinases and phosphatases and key signaling modules, such as the SH2 and SH3 domains, and the evolution of protein phosphorylation in prokaryotes and plants and how their systems differ from those in animals. A number of other topics, such as the functional conservation of orthologous proteins involved in phosphorylation, whether phosphorylation network architecture has been conserved, and the evolutionary function of conserved pseudokinases, would be discussed. Clearly for this topic it is particularly important to have as broad a representation as possible from the different areas of protein phosphorylation, we have selected speakers working on a wide range of eukaryotic and prokaryotic organisms in order to emphasize the evolution and conservation of protein phosphorylation.
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