The sessions in the "Protein Synthesis and Degradation" ASBMB annual meeting theme will cover the ribosome and protein translation, membrane protein biosynthesis, protein folding and quality control and protein aggregation and autophagy. The meeting will be held April 9-13, 2011, in Washington, D.C. (Titled "The Life of Proteins from Womb to Tomb" in print version.)
Most biochemical reactions depend on proteins whose precise abundance, conformation and location are critical. Thus, every step in a protein’s life, from its synthesis by ribosomes to culling by degradation pathways, is regulated tightly. Each of these four processes represents expansive fields on their own, and assembling a program to encompass everything proved challenging. The “Protein Synthesis and Degradation” theme aims to highlight some of the most recent frontiers in understanding how the life and death of proteins are regulated by the cell, as well as the importance of protein maturation and turnover pathways in the numerous human diseases related to protein misfolding, accumulation and aggregation.
Proteins begin their life as they emerge from inside ribosomes during their synthesis. In recent years, ribosomes have become known as far more than the protein synthetic machinery. They increasingly are appreciated as platforms for a wide range of protein maturation reactions. This includes co-translational modifications, initial interactions with chaperones and central roles in protein targeting. These co-translational reactions must be coordinated spatially and temporally and require the selective recruitment of various factors to the ribosome.
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The first session, titled “The Ribosome and Protein Translation” will investigate how this coordination is achieved. Shu-ou Shan (California Institute of Technology) will discuss biophysical analysis of how the signal recognition particle targeting pathway is regulated to ensure efficient and high fidelity delivery of nascent proteins to a cellular membrane. Nenad Ban (ETH Zurich) will describe how structural analysis of ribosome-associated factors is providing mechanistic insights to their function. Ramanujan S. Hegde (National Institutes of Health) will discuss new findings on understanding how a chaperone’s recruitment to ribosomes facilitates correct targeting of certain membrane proteins.