PULSe Home > Faculty Members A-C > Eric Barker

Assistant Professor of Med Chem Mol Pharm Ph.D. - 1997 - Vanderbilt University Contact Info: ericb@pharmacy.purdue.edu 765-494-9940 Training Group(s): Integrative Neuroscience

Current Research Interests:

rotransmitter transporters are responsible for removing neurotransmitters from the synapse and thus serve to "turn off" a chemical signal. These membrane proteins are also the targets for many clinically important drugs such as antidepressants, amphetamines, and cocaine. Our research is focused on understanding the molecular structure of these transporters and how structure relates to transport activity and drug recognition. Our studies on the antidepressant- and cocaine-sensitive serotonin transporter use molecular approaches such as chimeric transporters, site-directed mutagenesis, electrophysiology, and molecular modeling to identify domains of the transporter involved with the molecular actions of cocaine and the amphetamines. In addition to our studies on the serotonin transporter, we have characterized a distinct uptake process for endogenous marijuana-like substances known as endocannabinoids. The major endocannabinoid anandamide is transported by a facilitated process and we are seeking to identify the protein(s) involved with anandamide uptake. Presently, we are investigating the role of the enzyme, fatty acid amidohydrolase, and other fatty acid transport proteins in anandamide transport. Additional studies may lead to the cloning of novel proteins responsible for anandamide uptake. In summary, our studies will provide important new information about the structure/function of neurotransmitter transporters and lead to a better understanding of how drugs influence these proteins.

Selected Publications:

Rakhshan, F., Day, T.A., Blakely, R.D., and Barker, E.L. (2000). Carrier-mediated uptake of the endogenous cannabinoid anandamide in RBL-2H3 cells. J.Pharmacol.Exp.Ther. 292: 960-967.

Barker, E.L., Moore, K.R., Rakhshan, F. and Blakely, R.D. (1999). Transmembrane domain I contributes to the permeation pathway for serotonin and ions in the serotonin transporter. J. Neurosci. 19: 4701-4709.

Barker, E.L., Perlman, M.A., Adkins, E.M.., Houlihan, W.J., Pristupa, Z.B., Niznik, H.D., and Blakely, R.D. (1998). Antagonist binding sites on the serotonin transporter revealed by species-scanning mutagenesis: An aromatic residue in transmembrane domain I mediates species-specific recognition of mazindol and citalopram between human and Drosophila serotonin transporters. J.Biol.Chem. 273: 19459-19468.