Nael McCarty, Associate Professor
Ph.D., Cell Physiology, UT Health Science Center-Houston, 1990
Phone: (404) 385-2955
Fax: (404) 894-0519
Office: (Cherry Emerson) 223/230
Research Interests
Structure-function of ion channels, molecular physiology of cystic fibrosis, regulation of ion channels by synaptic proteins, human physiology. Ion channels and transporters in the plasma membrane play important roles in cellular physiology. They provide the pathways for movement of solutes across epithelia, such as in the kidney, and underlie signaling in excitable cells, such as neurons and myocytes.
Current Research
Ion channels in the plasma membrane play important roles in cellular physiology. They provide the pathways for movement of solutes across epithelia, such as in the kidney, and underlie signaling in excitable cells, such as neurons and myocytes. Modulation of ion channels often serves as the endpoints of signal transduction pathways involving hormones or neurotransmitters. Because these proteins carry electrical currents, they may be studied with exquisite resolution using electrophysiological techniques. Research in the laboratory of Professor Nael McCarty uses these approaches to study the structure of ion channels, and to study the regulation of channels and receptors in various cell types. The main focus of this work currently is on chloride channels, including the one that is defective in the lethal genetic disease, cystic fibrosis. The McCarty group's basic science studies aim to determine: a) the functional architecture of the chloride channel pore, and b) how this chloride channel is regulated in airway epithelial cells to control fluid secretion in the lung. The goal of the group's clinical studies is to help identify and develop new therapies for cystic fibrosis patients. In this way, these physiological studies span the range from individual molecules to human subjects.
Selected Publications
Zhang, Z.-R., S. Zeltwanger, S. S. Smith, D. C. Dawson, and N. A. McCarty. 2002. Voltage-sensitive gating induced by a mutation in the fifth transmembrane domain of CFTR. Am.J.Physiol. 282:L135-L145.
McCarty, N. A., and Z.-R. Zhang. 2001. Identification of a region of strong discrimination in the pore of CFTR. Am.J.Physiol. 281:L852-L867.
Smith, S. S., F. Sun, T. E. Kriewall, Z-R. Zhang, N. A. McCarty, and D. C. Dawson. 2001. CFTR: Covalent and non-covalent modification suggests a role for fixed charges in anion conduction. J. Gen. Physiol. 118:407-431.
McCarty, N. A. 2000. Permeation through the CFTR chloride channel. J.Exp.Biol. 203: 1947-1962.