July 2010

Meeting Theme: Protein Synthesis and Degradation

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.

Protein Folding

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).

Autophagy

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 (dikic@biochem2.uni-frankfurt.de) is director of the Institute of Biochemistry II at Goethe University Medical School. Ramanujan Hegde (hegder@mail.nih.gov) 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.

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