Applications for this meeting must be submitted by June 17, 2018. Please apply early, as some meetings become oversubscribed (full) before this deadline. If the meeting is oversubscribed, it will be stated here. Note: Applications for oversubscribed meetings will only be considered by the Conference Chair if more seats become available due to cancellations.
This meeting will focus on the foundational principles of thiol-based redox regulation and redox signaling. So far, we have come to understand that the function of a great many proteins is regulated by reversible thiol (or thioether) modifications. Sulfur transiently bonds to sulfur (disulfides and hydropersulfides), to oxygen (sulfenic acids, sulfoxides), and to nitrogen (sulfenyl amides, thionitrites). One key challenge is to understand how oxidative protein modifications are generated with specificity and efficiency. While thermodynamics defines the space of possibilities, kinetics dictates what actually happens. Thus, "thiol redox switching" is all about the controlled abatement of kinetic and diffusional barriers. Compartmentalization and supramolecular organization determine which redox partners get into contact which each other. Redox relays chains in which oxidizing or reducing equivalents are passed from one protein to another, long known in the context of oxidative protein folding, are now also seen to play a role in signaling. Relays require proximity and alignment between redox enzymes and their clients. This raises question of how redox enzymes and their redox-regulated target proteins recognize each other. Another key challenge is to understand the biological meaning of oxidative protein modifications. Central to this challenge is the ability to measure these modifications and their stoichiometry in vivo. This requires rigorous understanding of sulfur and reactive species chemistry. We also need to understand how thiol modifications integrate and cross-talk with other kinds of signaling. New insights inspire new tools: Chemical and genetic strategies to monitor and manipulate redox events increasingly exploit precise subcellular and supramolecular targeting. Genetic probes intercepting redox relays and proximity-directed chemical biology approaches are just two examples. The emerging tools offer exciting new opportunities, but we also need to discuss their limitations.
This GRC will be held in conjunction with the "Thiol-Based Redox Regulation & Signaling" Gordon Research Seminar (GRS)
. Those interested in attending both meetings must submit an application for the GRS in addition to an application for the GRC. Refer to the associated GRS program page
for more information.
The Conference will consist of nine sessions, on the topics listed below. The Conference Chair is currently developing their preliminary program, which will include the names of the invited speakers and discussion leaders for each of these sessions. The preliminary program will be available by November 15, 2017. Please check back for updates.
Keynote Session: New Paradigms in Redox Signaling
Making, Breaking and Re-Shuffling Disulfide Bonds in Oxidizing Compartments
Mechanisms of Redox Signaling: Non-Enzymatic Thiol Oxidation
Mechanisms of Redox Signaling: Enzymatic Thiol Oxidation
Reactive Oxygen and Nitrogen Species: Generation, Trafficking and Function
Reactive Sulfur Species: Generation, Trafficking and Function
Metabolism, NAD(P)H Status and Redox Signaling
Case Studies on Redox-Regulated Proteins in the Physiological Context
Tools and Strategies to Monitor, Enhance or Interrupt Redox Signals