Meeting Program

To view program in "24 hour" time (international) click here.

Sunday, January 23
3:00 - 7:30 PM	Registration	Longs Peak Foyer
6:30 - 7:30 PM	Refreshments	Longs Peak Foyer
7:30 - 8:30 PM	Keynote Address Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Tony Pawson, Samuel Lunenfeld Research Institute, Canada Evolution of Tyrosine Kinase-Based Signaling
Monday, January 24
7:00 - 8:00 AM	Breakfast	Quandary Peak
8:00 - 11:00 AM	Bioinformatics of Protein Phosphorylation Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Gerard Manning, The Salk Institute, USA Kinome Evolution
	Rune Linding, Institute of Cancer Research (ICR), UK Evolution of Complex Regulatory Systems - Signaling Fidelity and Disease
	Nicholas K. Tonks, Cold Spring Harbor Laboratory, USA Signal Transduction from a Protein Tyrosine Phosphatase Perspective
	James E. Ferrell Jr., Stanford University, USA Bistable Kinase Networks
	Matthew P. Jacobson, University of California, San Francisco, USA Short Talk: Computational Studies of Protein Regulation by Post-Translational Phosphorylation
9:20 - 9:40 AM	Coffee Break	Longs Peak Foyer
11:15 AM- 1:00 PM	Poster Setup	Quandary Peak
1:00 - 10:00 PM	Poster Viewing	Quandary Peak
4:30 - 5:00 PM	Coffee Available	Longs Peak Foyer
5:00 - 7:00 PM	Phosphoproteomics Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Steven P. Gygi, Harvard Medical School, USA Cell Cycle Phosphoproteomics
	Rudolf H. Aebersold, Institute of Molecular Systems Biology, ETH Zurich, Switzerland Talk Title to be Determined
	Judit Villen, Harvard Medical School, USA Short Talk: Yeast Phosphoproteome
	Philip A. Cole, Johns Hopkins University School of Medicine, USA Talk Title to be Determined
7:00 - 8:00 PM	Social Hour w/ Lite Bites	Quandary Peak
7:30 - 10:00 PM	Poster Session 1 Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Quandary Peak
Tuesday, January 25
7:00 - 8:00 AM	Breakfast	Quandary Peak
8:00 - 11:00 AM	Phosphorylation Networks Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Nevan J. Krogan, University of California, San Francisco, USA Comparative Analysis of Protein Phosphorylation Networks in Fungi
	Stephen W. Michnick, Université de Montréal, Canada Functional Constraints on Phosphoproteomes
	Michael Tyers, University of Edinburgh, UK Global Architecture of the Kinase-Phosphatase Interaction Network
	Michael B. Yaffe, Massachusetts Institute of Technology, USA DNA Damage Signaling Networks
9:20 - 9:40 AM	Coffee Break	Longs Peak Foyer
11:00 AM- 1:00 PM	Poster Setup	Quandary Peak
1:00 - 10:00 PM	Poster Viewing	Quandary Peak
4:30 - 5:00 PM	Coffee Available	Longs Peak Foyer
5:00 - 7:00 PM	Evolution of Tyrosine Phosphorylation Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Piers Nash, University of Chicago, USA Short Talk: SH2 Domain Linguistics and the Evolution of Selective Interactions
	Wendell A. Lim, University of California, San Francisco, USA Evolution of Tyrosine Kinase-Based Signaling
	Bruce J. Mayer, University of Connecticut Health Center, USA Evolution of Complex Signaling Machinery
	Speaker to be Announced,
7:00 - 8:00 PM	Social Hour w/ Lite Bites	Quandary Peak
7:30 - 10:00 PM	Poster Session 2 Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Quandary Peak
Wednesday, January 26
7:00 - 8:00 AM	Breakfast	Quandary Peak
8:45 - 11:00 AM	Evolution of Prokaryotic Protein Kinases Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Tom Alber, University of California, Berkeley, USA Ser/Thr Phosphosignaling in TB
	Christophe Grangeasse, CNRS - University of Lyon, France Short Talk: Bacterial Tyrosine Kinases
	Ann M. Stock, University of Medicine and Dentistry of New Jersey, USA Mechanistic Diversity in Bacterial Two-Component Signaling Systems
	Michael T. Laub, Massachusetts Institute of Technology, USA Specificity and Evolution of Two-Component Signaling Pathways
	Andrew Xiao, Yale University, USA Short Talk: WSTF Coordinates Transcription and DNA Damage Repair during Development
9:20 - 9:40 AM	Coffee Break	Longs Peak Foyer
11:00 AM- 1:00 PM	Poster Setup	Quandary Peak
1:00 - 10:00 PM	Poster Viewing	Quandary Peak
4:30 - 5:00 PM	Coffee Available	Longs Peak Foyer
5:00 - 7:00 PM	Protein Kinase Medley Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Shin-Han Shiu, Michigan State University, USA Birth and Death Evolution of Protein Kinases in Plants
	Christian Doerig, École Polytechnique Fédérale de Lausanne, Switzerland The Kinome of Malaria Parasites
	Edward Y. Skolnik, New York University Medical Center, USA Short Talk: Histidine Kinases
	Natalie G. Ahn, University of Colorado, USA Talk Title to be Determined
7:00 - 8:00 PM	Social Hour w/ Lite Bites	Quandary Peak
7:30 - 10:00 PM	Poster Session 3 Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Quandary Peak
Thursday, January 27
7:00 - 8:00 AM	Breakfast	Quandary Peak
8:00 - 11:00 AM	Evolution of Protein Structures Used in Phosphorylation Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Susan S. Taylor, University of California, San Diego, USA Evolution of the Protein Kinase Catalytic Domain
	Stefan Knapp, University of Oxford, UK Lessons Learned from Wide-Scale Protein Kinase Structure Determination
	Louise N. Johnson, University of Oxford, UK Protein Kinase Inhibitors: Contributions from Structure to Clinical Compounds
	Zongchao Jia, Queen's University, Canada Short Talk: Structures of E. coli Bifunctional Isocitrate Dehydrogenase Kinase/ Phosphatase and its Complex with Isocitrate Dehydrogenase
	Natarajan Kannan, University of Georgia, USA Short Talk: Structural Constraints in the Protein Kinase Catalytic Domain
9:20 - 9:40 AM	Coffee Break	Longs Peak Foyer
11:00 AM- 1:00 PM	Poster Setup	Quandary Peak
1:00 - 10:00 PM	Poster Viewing	Quandary Peak
4:30 - 5:00 PM	Coffee Available	Longs Peak Foyer
5:00 - 7:00 PM	Phosphatase Evolution Registered attendees for this meeting can view Abstracts for this session starting on 12/23/2010	Longs/Grays Peaks
	Jack E. Dixon, University of California, San Diego, USA Phosphatomes
	Tricia Cohen, University of Dundee, UK Serine/Threonine Protein Phosphatase Families
	Anne-Claude Gingras, Samuel Lunenfeld Research Institute, Canada Phosphoproteomics of Protein Phosphatase Complexes
8:00 - 11:00 PM	Entertainment	Quandary Peak
Friday, January 28
	Departure
*=Session Chair     †=Speaker invited, not yet responded.

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.