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.
Membrane Protein Biosynthesis
Protein folding and maturation has long been a challenging scientific topic. Within this area, complex membrane proteins are especially difficult to investigate because of their hydrophobicity and need to insert and fold in the context of a lipid bilayer. The session, titled “Membrane Protein Biosynthesis,” will explore the insights into how complex membrane proteins are made and assembled properly.
Protein Synthesis and Degradation
Session: The Ribosome and Protein Translation
• Coordination of Translation and Protein Targeting, Shu-ou Shan, California Institute of Technology
• Structure and Function of Ribosome-associated Factors, Nenad Ban, ETH Zurich
• Ribosome-associating Chaperones in Membrane Protein Insertion, Ramanujan S. Hegde, National Institutes of Health
Session: Membrane Protein Biosynthesis
• In Vivo Kinetics of Membrane Protein Integration, Reid Gilmore, University of Massachusetts Medical School
• Cellular Mechanisms of Polytopic Protein Folding, William Skach, Oregon Health and Science University
• Using High Content Microscopy Screening to Uncover Novel Insertion Pathways for Transmembrane Proteins, Maya Schuldiner, Weizmann Institute of Science
Session: Protein Folding and Quality Control
• Mechanisms of Cytosolic Chaperone Function, Elizabeth A. Craig, University of Wisconsin-Madison
• Mechanisms of ER-associated Protein Degradation, Yihong Ye, National Institutes of Health
• Chaperone-mediated Protein Folding and Disease, Arthur L. Horwich, Investigator, Howard Hughes Medical Institute, Yale University School of Medicine
Session: Protein Aggregation and Autophagy
• Ubiquitin and Autophagy Networks,
Ivan Dikic, Goethe University Medical School
• Autophagy in Physiology and Disease, Beth Levine, University of Texas Southwestern Medical Center
• Mechanisms Underlying Protein Aggregation and Autophagy, Anne Simonsen, Oslo University
Reid Gilmore (University of Massachusetts Medical School) will describe a novel application of in vivo methods to examine the kinetics of how successive transmembrane segments of a multispanning membrane protein are inserted during synthesis. William Skach (Oregon Health and Science University) will describe the use of biophysical in vitro methods to probe the interplay between membrane protein insertion and folding. Maya Schuldiner (Weizmann Institute of Science) will discuss how large-scale genome approaches combined with microscopy can uncover new components and pathways of membrane insertion.
The session “Protein Folding and Quality Control” will focus on chaperones and their dual roles in facilitating substrate folding on the one hand and mediating quality control on the other. Elizabeth A. Craig (University of Wisconsin-Madison) will describe her efforts to understand the molecular basis of how chaperone diversity allows their wide-ranging functional properties. Yihong Ye (National Institutes of Health) will focus on quality control pathways involved in degrading misfolded proteins from the endoplasmic reticulum. And, finally, chaperone-mediated folding and its role in diseases of protein misfolding will be discussed by Arthur L. Horwich (Investigator, Howard Hughes Medical Institute, Yale University School of Medicine).
Degradation pathways that are both selective and nonselective are critical to the maintenance of protein homeostasis. Autophagy has emerged as being important in a wide range of degradation processes from specific proteins to whole organelles. The session “Protein Aggregation and Autophagy” will explore the role of autophagy in clearing terminally misfolded and aggregated proteins.
Ivan Dikic (Goethe University Medical School) will discuss his studies on the relationship of ubiquitin pathways to the regulation of selective autophagy processes. Beth Levine (University of Texas Southwestern Medical Center) will describe the physiologic functions of autophagy and its misregulation in disease. In addition, understanding how autophagy controls the metabolism of protein aggregates will be explained by Anne Simonsen (Oslo University).
When buttressed with 12 short talks selected from abstracts, this theme will provide a cross-sectional view of several of the most active areas in understanding the complex and regulated life of proteins. By combining talks that span a range of methods, experimental systems and topics, the sessions should stimulate new ideas and directions for future studies.
Ivan Dikic (email@example.com) is director of the Institute of Biochemistry II at Goethe University Medical School. Ramanujan Hegde (firstname.lastname@example.org) is head of the protein biogenesis section of the cell biology and metabolism program at the National Institute of Child Health and Human Development, National Institutes of Health.