Matthias Quick, Ph.D.
Associate Professor of Neurobiology (in Psychiatry) and Physiology and Cellular Biophysics
Molecular mechanism of integral membrane proteins
Matthias Quick was trained in microbiology, molecular biology, physiology, and neurobiology, and many of his multidisciplinary research projects are conducted in collaboration with leading experts in the field of computational biophysics, spectroscopy, genetics, and structural studies. He is currently Associate Professor of Neurobiology (in Psychiatry) and in the Department of Physiology and Cellular Biophysics and Research Scientist in the New York State Psychiatric Institute (NYSPI) Division of Molecular Therapeutics. He also serves as the Director of Laboratory Operations and Safety in CU Psychiatry, NYSPI, and RFMH.
His research interests center around the molecular mechanism of integral membrane proteins with special emphasis on secondary transporters. The long-term goal of the research in his lab is to decipher the mechanism of these molecular machines at the molecular level to gain insight into their role in various physiological and pathophysiological processes and how drugs interfere with their activity. Current research focuses on the following areas:
1) Elucidation of the structure, function and dynamics of Na+-coupled transporters (symporters). Special emphasis is given to i) neurotransmitter:sodium symporters (NSS) and ii) solute:sodium symporters (SSS).
2) Characterization of the molecular mechanism of the Plasmodium falciparum chloroquine transporter (PfCRT). The goal of this study, that is conducted in close collaboration with CUIMC colleagues Drs. Fidock and Mancia, is to elucidate the role of PfCRT in malaria drug resistance and physiological context.
3) Development of new technologies to characterize membrane protein function. Using newly developed technologies, involving radiotracer-based and electrophysiological transport and binding studies in reconstituted systems, the Quick lab is currently performing studies on vesicular transporters, antiporters, channels, and receptors implicated in human diseases.
Focht, D, Neumann, C, Lyons, J, Bilbao, AE, Blunck, R, Malinauskaite, L, Schwarz, IO, Javitch, JA, Quick, M, Nissen, P. A non-helical region of transmembrane helix 6 of hydrophobic amino acid transporter MhsT mediates substrate recognition. EMBO J, 2021; 40:e105164
Quick, M, Dwivedi, M, Padan, E. Insight into the direct interaction of Na+ with NhaA and mechanistic implications. Sci Rep, 2021; 11:7045
Fitzgerald, GA, Terry, DS, Warren, AL, Quick, M, Javitch, JA, Blanchard, SC. Single-molecule recordings of secondary transporter activity with single-turnover resolution. Nature, 2019; 575:528-534
Kim, J, Tan, YZ, Wicht, KJ, Erramilli, SK, Dhingra, SK, Okombo, J, Vendome, J, Hagenah, LM, Giacometti, SI, Warren, AL, Nosol, K, Roepe, PD, Potter, CS, Carragher, B, Kossiakoff, AA, Quick, M, Fidock, DA, Mancia, F. Structure and drug resistance properties of the Plasmodium falciparum transporter PfCRT. Nature, 2019; 576:315-320
Zehnpfennig, B, Wiriyasermkul, P, Carlson, D, Quick, M. Interaction of α-lipoic acid with the human Na+/multivitamin transporter (hSMVT). J Biol Chem, 2015; 290:16372-16382
Zhou, X, Levin, EJ, Pan, Y, McCoy, JG, Sharma, R, Kloss, B, Bruni, R, Quick, M, Zhou, M. Structural basis of the alternating-access mechanism in a bile acid transporter. Nature, 2014; 505:569-573
Malinauskaite, L, Quick, M, Reinhard, L, Lyons, JA, Yano, H, Javitch, JA, Nissen, P. A mechanism for intracellular release of Na+ by neurotransmitter/sodium symporters. Nat Struct Mol Biol, 2014; 21:1006-1012
Quick, M, Shi, L, Zehnpfennig, B, Weinstein, H, Javitch, JA. Experimental conditions can obscure the second high-affinity site in LeuT. Nat Struct Mol Biol, 2012; 19:207-211
Delmondes de Carvalho, F, Quick, M. Surprising substrate versatility in SLC5A6: Na+-coupled I- transport by the human Na+/multivitamin transporter (hSMVT). J Biol Chem, 2011; 286:131-137
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