Dorit Ron, Ph.D.
Associate Professor of Neurology

Contact Information:
Dorit.Ron@ucsf.edu
Tel: (510) 985-3150
Fax: (510) 985-3101
5858 Horton Street
Suite 200
Emeryville, CA 94608


Links:
lab website

Ernest Gallo Clinic & Research Center

Molecular neurobiology of addiction

My laboratory is interested in understanding the molecular mechanisms that underlie alcohol addiction. Alcoholism is a devastating and costly disease, but unfortunately very few medications are available to treat adverse phenotypes such as craving and relapse. Understanding how alcohol exerts its short- and long-term actions on the brain is therefore highly important. We use molecular and electrophysiological approaches in parallel with behavioral models to study how acute and prolonged exposure of neurons to ethanol alters normal functions, and test the behavioral consequences to these changes in rodents. For the past several years we have been concentrating our efforts on the actions of ethanol on the ligand-gated ion channel NMDA, and the growth factors BDNF and GDNF.

Selected Publications:
McGough N. N. H., He D.-Y., Janak P. H., Phamluong, K., Janak P. H., Ron D. RACK1 and BDNF: A homeostatic pathway that regulates alcohol addiction. J. Neuroscience, 2004, In press.

Ron, D., Signaling Cascades Regulating NMDA Receptor Sensitivity to Ethanol. (Review) Neuroscientist, Aug;10(4):325-336, 2004.

Thornton, C., Tang, K.-C., Phamluong, K., Luong, K., Vagts, A., Nikanjam, D., Yaka, R., and Ron, D. Spatial and temporal regulation of RACK1 function and NMDA receptor activity through WD40 motif-mediated dimerization. Journal of Biological Chemistry, 279(30): p. 31357-31364, 2004.

Yaka, R., Tang, K.-C., Camarini, R., Janak, P.H., and Ron, D. Fyn kinase and NR2B containing NMDA receptors regulate acute ethanol sensitivity but not intake or conditioned reward. Alcoholism: Clinical and Experimental Research, 27(11): p. 1736-1742, 2003.

Vagts, A.J., He, D.-Y., and Ron, D. Cellular adaptation to chronic ethanol results in altered compartmentalization and function of the scaffolding protein RACK1. Alcoholism: Clinical and Experimental Research, 27(10): p. 1599-1605, 2003.

Ungless, M., Singh, V., Crowder, T.L., Yaka, R., Ron, D., and Bonci, A. Corticotropin-releasing factor (CRF) requires CRF-binding protein to potentiate NMDA receptors via CRF receptor 2 in dopamine neurons. Neuron. 39, 401-407, 2003.

Thornton, C., Yaka, R., Dinh, S. and Ron, D. H-Ras Modulates N-Methyl-D-aspartate Receptor Function via Inhibition of Src Tyrosine Kinase Activity Journal of Biological Chemistry, 278(26): p. 23823-23829, 2003.

Yaka, R., Phamluong, K. and Ron, D. Scaffolding of Fyn Kinase to the NMDA Receptor Determines Brain Region Sensitivity to Ethanol. J. Neuroscience 23(9): p. 3623-3632, 2003.

Yaka, R., He, D.Y., Phamluong, K. and Ron, D. Pituitary adenylate cyclase activating polypeptide (PACAP 1-38) enhances NMDA receptor function and BDNF expression via rack. Journal of Biological Chemistry, 278(11): p. 9630-9638, 2003.

He, D.Y., Vagts, A.J., Yaka, R. and Ron, D. Ethanol Induces Gene Expression via Nuclear Compartmentalization of Receptor for Activated C Kinase 1. Molecular Pharmacology 62(2): p. 272-280, 2002.

Yaka, R., Thornton, C., Vagts, A.J., Phamluong, K., Bonci, A., and Ron, D. NMDA-receptor function is regulated by the inhibitory scaffolding protein RACK1. Proceedings of the National Academy of Sciences 99: 5710-5715, 2002.

Ron, D., Vagts, A.J., Dohrman, D. P., Yaka, R., Jiang, Z., Yao, L., Crabbe, J., Grisel, J.E. and Diamond, I. Uncoupling of bIIPKC from its targeting protein RACK1 in response to ethanol in cultured cells and mouse brain. FASEB Journal, 14: 2303-2314, 2000.

Ron, D., Jiang, Z., Yao, L., Vagts, A.J., Diamond, I., Gordon, A.S. Coordinated movement of RACK1 with activated bIIPKC. Journal of Biological Chemistry 274: 27039-27046, 1999.

Ron, D., Napolitano, E. W., Voronova, A., Vasquez, N.J., Roberts, D.N., Calio, B.L., Caothien, R.H., Pettiford, S.M., Wellik, S., Mandac, J.B., Kauvar, L. Direct interaction in T-cells between PKC and the Tyrosine Kinase p59fyn. Journal of Biological Chemistry 274: 19003-19010, 1999.

Ron, D. and Kazanietz, M.G. New insights of Protein Kinase C and novel Phorbol Ester Receptors. FASEB Journal 13: 1658-1676,1999.

Rodriguez, M., Ron, D., Kazushige, T., Chen, C.-H., Mochly-Rosen, D. RACK1, a Protein Kinase C anchoring protein coordinates the binding of activated Protein Kinase C and select pleckstrin homologydomains in vitro. Biochemistry 38: 13787-13794, 1999.

Yedovitzky, M., Mochly-Rosen, D., Ron, D., Gray, M. O., Johnson, J. A., Abramovitch, E., Cerasi, E., and Nesher, R. Translocation inhibitors define specificity of protein kinase C isozymes in pancreatic beta cells. Journal of Biological Chemistry (Communication) 272: 1417-1420, 1997.

Ron, D., Luo, J., and Mochly-Rosen, D. C2 region-derived peptides inhibit translocation and function of beta protein kinase C in vivo. Journal of Biological Chemistry 270: 24180-7, 1995.

Ron, D., and Mochly-Rosen, D. A new autoregulatory region in protein kinase C - the pseudo-RACK binding site. Proceedings of the National Academy of Sciences 92: 492-496, 1995.

Ron, D., and Mochly-Rosen, D. Agonists and antagonists of protein kinase C function, derived from its binding proteins. Journal of Biological Chemistry (Communication) 269: 21395-21398, 1994.

Ron, D., Chen, C. H., Caldwell, J., Jamieson, L., Orr E., and Mochly-Rosen, D. Cloning of an intracellular receptor for protein kinase C: a homolog of the beta subunit of G proteins. Proceedings of the National Academy of Sciences 91: 839-43, 1994.