The production, sorting and selection of newly synthesized proteins in eukaryotes
Proteins possess a mind-boggling array of activities, but before they perform their diverse functions, they must be synthesized and fold with high fidelity. During or after synthesis, about one-third of all newly synthesized eukaryotic proteins enter the secretory pathway and therefore also must be transported into the endoplasmic reticulum, where they fold and are post-translationally modified. Secreted proteins that are improperly synthesized, transported or processed are recognized by components of a quality-control machinery that targets them for degradation. Because so many things can go wrong during the early life of a protein, it comes as no surprise that a significant number of human diseases are linked to protein biogenesis.
The four sessions in the “Protein Synthesis, Targeting and Quality-Control” theme will provide an overview and detail cutting-edge methods and discoveries related to these topics.
The ribosome and early folding decisions
Proteins start their lives at the ribosome. From here, they must begin the complicated process of folding and being transported to their final destinations. This session will highlight our current mechanistic understanding of early steps in protein biogenesis.
Jody Puglisi (Stanford University School of Medicine) has pioneered the use of single-particle studies to understand the dynamics of protein synthesis, directly visualizing independent components during the translation cycle.
Wolfgang Wintermeyer (Max Planck Institute for Biophysical Chemistry in Göttingen) also will speak to the dynamics of the translation process, focusing on the nascent chain and its interactions.
Walid Houry (University of Toronto) will illuminate the roles of some of the ribosome’s partners, specifically discussing the role of chaperone assemblies.