Membrane Structure and Assembly
Membrane Structure Perturbation and Disassembly
This is the working title of the upcoming symposium of the Membrane Structure and Assembly Subgroup in Philadelphia, during the 2013 Annual Meeting. A better understanding of these phenomena is of major importance for a broad range of fields, all the way from antimicrobial peptides and membrane-active drugs to the solubilisation of membrane proteins by detergents.
Tom Thompson has been invited to present the first Thomas E. Thompson Award to Bill Wimley, Tulane University. The award is sponsored by Avanti Polar Lipids. After Bill’s award lecture, Alan Grossfield, Rochester University and Ole Mouritsen, Odense University, Denmark, will speak about aspects of membrane structure perturbation. After the break, Erwin London, Stony Brook University; Sandro Keller, University of Kaiserslautern, Germany; and Klaus Gawrisch, NIH, will address topics related to the solubilisation and reconstitution of membrane components.
See you in Philadelphia!
—Heiko Heerklotz, Chair, MSA Subgroup
Postdoctoral Research Award
Postdoctoral researchers working on intrinsically disordered proteins may compete for one of two Postdoctoral Research Awards which will include an honorarium and an opportunity to present a short talk at the 2013 IDP Subgroup Symposium. Send your submitted abstract (regular or late) and its BPS abstract control number, via email to IDPsymposium2013@gmail.com. To be eligible you must be a postdoctoral researcher at the time of abstract submission and have your advisor confirm this via email to IDPsymposium2013@gmail.com. The deadline to apply is December 14! Functional Mechanisms of IDPs We continue our series of contributions covering broad aspects of the IDP field with a brief overview of functional mechanisms for which IDPs have evolved. Since the very first reports of functional IDPs, the ability of portions of these proteins to fold upon binding to their interaction partners has been evident. This feature is observed in all the realms of life, from proteins involved in the assembly of bacterial flagella to cell cycle regulators and transcription factors in eukaryotes. Coupled binding and folding allows certain IDPs to bind diverse partners by assuming different conformations, and permits high binding specificity without high affinity. Both features are consistent with the role of IDPs as hub proteins in signaling pathways.
Intriguingly, many other functions of IDPs do not require folding. Some IDPs may bind their partners in a ‘fuzzy’ fashion, exhibiting multiple interaction regions that rapidly exchange for binding to a single site on their partners. Recently, disordered segments have been shown to modulate solution-gel phase transitions of protein assemblies implicated in cell signaling events. While disordered proteins are more common within higher organisms, every form of life takes advantage of the unique functional characteristics bestowed by the lack of tertiary structure. Disorder regions are key regulators of the assembly-disassembly of viral particles; they are responsible for the amazing mechanical properties of spider silk and play the role of gatekeepers in the nuclear pore complex of eukaryotes. Even at this early stage, it is evident that intrinsic disorder is crucial to the performance of diverse and fascinating biological functions.
—Ariele Viacava Follis, Postdoc Representative, IDP Subgroup
December 2012 Table of Contents