Vinzenz M Unger, Ph.D.
Professor; Northwestern University, Dept of Molecular Biosciences
Education
1991 Diploma in Biochemistry, Tübingen University/Germany
1995 PhD in Biochemistry, Cambridge University/UK
Professional Experience
1998-2000 Group Leader; Max-Planck Institute for Biophysics, Dept. of Structural Biology,
Frankfurt/Germany
2000-2004 Assistant Professor; Yale University, Dept. of Molecular Biophysics and Biochemistry,
New Haven, CT
2005-2010 Associate Professor; Yale University, Dept. of Molecular Biophysics and Biochemistry,
New Haven, CT
6/2010- Professor; Northwestern University, Dept of Molecular Biosciences, Evanston, IL
Topic：In the Shadows of the Membrane - An Emerging Tale about How to Beat the Odds in Cellular Copper Acquisition
Abstract:
Due to their redox and coordination properties, ions of the transition metal copper are essential for life, partaking in critical cellular processes like respiration, antioxidant defense, neurotransmitter synthesis and the formation of connective tissue. While being essential, the same properties that make copper ions useful also are potentially dangerous because uncontrolled formation of radicals can impart significant damage and cell death. Facing this dual nature of copper ions, cells have developed intricate mechanisms that carefully control the movement of copper ions from the moment they enter our bodies. Owing to structural biology, much is known about the structures of copper binding proteins, and the mechanisms by which copper ions are transferred from cellular copper chaperones to downstream targets that require copper for function. Contrasting with this wealth of knowledge, the mechanisms underlying cellular copper uptake and initial intracellular distribution are only beginning to emerge. In this seminar, I will describe the progress that we have made over the past 13 years in solving the structure of the human high-affinity copper transporter hCTR1, and how this structure has guided us to the paradigm shifting discovery that intracellular copper chaperones exploit the membrane as a scaffold to facilitate direct molecular interactions between the chaperone and the copper uptake transporter.
Venue: Room143, New Biology Building, THU
Time: May 21 (Tuesday), 2013; 16:30
Host: Prof. Hongwei Wang
