Robert A. Farley
Professor Physiology and Biophysics, Biochemistry and Molecular Biology
Research Topics
- Na, K-ATPase
- Neurotransmitter transport
- Peptide transport
- Protein structure
- Membrane proteins
Research Overview
The primary interest of our lab is to understand the mechanisms that cells have developed to move ions and small molecules across cell membranes. Ion gradients of sodium and potassium underlie all electrical activity in cells, and much of our work deals with the structure and mechanism of Na,K-ATPase, which is the protein that catalyzes the active transport of these ions, and establishes and maintains their gradients. In another project, we are investigating the mechanism of serotonin transport by the serotonin transporter. The serotonin transporter is a member of a class of proteins that couple neurotransmitter uptake to the transport of sodium, chloride, and potassium, and we are working to understand how the interaction among these different substrates for the protein lead to their transport. A third area of interest in our lab is the transport of small peptides across the intestinal epithelium. The transporter for peptides, PepT1, recognizes and transports all combinations of di- and tri-peptides, making it an attractive target for prodrug development designed to facilitate oral delivery of pharmaceuticals. Our research into the structure and mechanisms of transport of each of these transporters utilizes techniques of membrane protein biochemistry, electrophysiology, and molecular biology.Contact Information
- E-mail:
- rfarley@usc.edu
- Office Location:
- MMR 250
- Office Phone:
- (323) 442-1240
- Lab Location:
- MMR 213
- Fax:
- (323) 442-2283
Education
- B.A., Hofstra University, 1970.
- Ph.D., University of Rochester, 1975.
Research Images
Selected Publications
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Pyrko P, Kardosh A, Liu YT, Soriano N, Xiong W, Chow RH, Uddin J, Petasis NA, Mircheff AK, Farley RA, Louie SG, Chen TC, Schonthal AH. (2007) Calcium-activated endoplasmic reticulum stress as a major component of tumor cell death induced by 2,5-dimethyl-celecoxib, a non-coxib analogue of celecoxib. Mol Cancer Ther. 6(4):1262-75. -PubMed
Nagy AK, Kane DJ, Tran CM, Farley, RA, and Faller LD. (2005) Evidence calcium pump binds magnesium before inorganic phosphate. J. Biol. Chem. 280: 7435-7443. -PubMed
Xu G, Kane DJ, Faller LD, and Farley RA. (2004) The role of loop 6/7 in folding and functional performance of Na,K-ATPase. J. Biol. Chem. 279: 45594-45602. -PubMed
Faller LD, Nagy AK, Kane DJ, and Farley RA. (2003) Mechanism of phosphoryl group transfer. Ann. N.Y. Acad. Sci. 986: 275-277. -PubMed
Li M, Farley RA, and Lester HA. (2002) Voltage-dependent transient currents of human and rat 5-HT transporters (SERT) are blocked by HEPES and ion channel ligands. FEBS Lett. 513: 247-252. -PubMed
Muller-Ehmsen J, Juvvadi P, Thompson CB, Tumyan L, Croyle M, Lingrel JB, Schwinger RH, McDonough AA, and Farley RA. (2001) Ouabain and substrate affinities of human Na,K-ATPase alpha(1)beta(1), alpha(2)beta(1), and alpha(3)beta(1) when expressed separately in yeast cells. Am. J. Physiol. Cell Physiol. 281: C1355-C1364. -PubMed
Wang J, Velotta JB, McDonough AA, and Farley RA. (2001) All human Na(+)-K(+)-ATPase alpha subunit isoforms have a similar affinity for cardiac glycosides. Am. J. Physiol. Cell Physiol. 281: C1336-C1343. -PubMed
Farley RA, Elquza E, Muller-Ehmsen J, Kane DJ, Nagy AK, Kasho VN, and Faller LD. (2001) 18O-exchange evidence that mutations of arginine in a signature sequence for P-type pumps affect inorganic phosphate binding. Biochemistry 40: 6361-6370. -PubMed
Farley RA, Schreiber S, Wang SG, and Scheiner-Bobis G. (2001) A hybrid between Na(+)-K(+)-ATPase and H(+)-K(+)-ATPase is sensitive to palytoxin, ouabain, and SCH28080. J. Biol. Chem. 276: 2608-2615. -PubMed
Li M, Farley RA, and Lester HA. (2000) An intermediate state of the gamma-aminobutyric acid transporter GAT1 revealed by simultaneous voltage clamp and fluorescence. J. gen. Physiol. 115: 491-508. -PubMed