Matthias Quick, Ph.D.
Assistant Professor of Neurobiology (in Psychiatry) at CUMC
Research Scientist V,
New York State Psychiatric Institute
Matthias Quick, Ph.D. is Assistant Professor of Clinical Neurobiology (in Psychiatry) in the Department of Psychiatry and in the Center for Molecular Recognition in the Columbia University College of Physicians and Surgeons, and Research Scientist V in the New York State Psychiatric Institute Division of Molecular Therapeutics.
He was educated in Germany where he obtained his B.S. (1991) and M.S. (1995) in Biology, and his Ph.D. in Microbiology/Membrane Transport (1998) at the University of Osnabrück. During his graduate work under the supervision of Dr. Heinrich Jung he developed several tools that aided in the functional and structural characterization of Na+-dependent symporters. After his graduation, Dr. Quick did postdoctoral work on the human Na+/glucose transporter (hSGLT1) in the laboratory of Dr. Ernest Wright FRS in the Department of Physiology at the David Geffen School of Medicine at UCLA where, in addition to the functional characterization of this protein with electrophysiological methods, he established the functional expression of recombinant hSGLT1 in bacteria. Dr. Quick joined the Center for Molecular Recognition in 2003 where, together with Dr. Jonathan Javitch, he studied the structure and function relationship of members of the neurotransmitter:sodium symporter (NSS) family. In 2008 he was appointed to the Faculty of the Department of Psychiatry. His work has substantially contributed to our better understanding of the molecular event underlying Na+-coupled transport processes.
Undergraduate: University of Osnabrueck, MS, 1989-1995
Graduate: University of Osnabrueck, PhD, 1995-1998
Fellowship: David Geffen School of Medicine at UCLA, 1999-2000
Post-Graduate: David Geffen School of Medicine at UCLA, 2000-2003
NYSPI Kolb Annex
Room 359 Unit/Box:25
1051 Riverside Drive
New York, NY 10032
Structure, function and dynamics of Na+-coupled transporters (symporters) with special emphasis on neurotransmitter:sodium symporters, the molecular targets for antipsychotic drugs and psychostimulants
1. Quick, M & Javitch, JA: Monitoring the activity of membrane transport proteins in detergent-solubilized form. Proc Natl Acad Sci USA 2007;104: 3603-3608
2. Shi, L*, Quick, M*, Zhao, Y, Weinstein, H & Javitch JA: The mechanism of a neurotransmitter:sodium symporter – inward release of Na+ and substrate is triggered by substrate in a second binding site. Mol Cell 2008;30: 667-677
3. Quick, M*, Lund Winther, AM*, Shi, L*, Nissen, P, Weinstein, H & Javitch, JA: Binding of an octylglucoside detergent molecule in the second substrate (S2) site of LeuT establishes an inhibitor-bound conformation. Proc Natl Acad Sci USA 2009;106: 5563-5568
4. Levin, EJ, Quick, M & Zhou, M: Crystal structure of a bacterial homolog of the kidney urea transporter. Nature 2009;462: 757-761
5. Quick, M, Shi, L, Zehnpfennig, B, Weinstein, H & Javitch, JA: Experimental conditions can obscure the second high-affinity site in LeuT. Nature Struct Mol Biol 2012;19: 207-211