Shelley Hooks, Ph.D.
Pharmaceutical and Biomedical Sciences
|Ph.D. Biochemistry||University of Virginia||Charlottesville, VA||2000|
|B.S. Biochemistry||Clemson University||Clemson, SC||1996|
- Post-doctoral Experience
- Postdoctoral Fellow, University of North Carolina-Chapel Hill, Chapel Hill, NC, 2001-2004
- Honors and Awards
- Awarded individual postdoctoral F32 NRSA grant (NIGMS), 2002
Founded and organized UNC Women in Science and Research, 2001-2004
Won oral communication award at the Western Pharmacology Society conference, 1999
Awarded individual predoctoral F31 NRSA grant from NIH (NIDA), 1999
Appointed to Cell and Molecular Biology training grant, 1997
Awarded Clemson Scholars scholarship, 1992-1996
- Research Interests
- Research focuses on the dynamic regulation of heterotrimeric G-proteins by transmembrane G-protein coupled receptors (GPCRs) and multifunctional Regulator of G-protein Signaling (RGS) proteins. There is a broad interest in defining the molecular mechanisms that govern the physiologic impact of these signaling complexes. A primary interest is the multi-domain striatal RGS protein, RGS9-2, which regulates dopamine receptor signaling. Alterations in dopamine receptor activity in the striatum are implicated in the development of drug addition and Parkinson’s disease. The ability of RGS9-2 to modulate cellular responses to dopaminergic signaling suggests that RGS9-2 may be a therapeutic target in the treatment of these pathologies. Specific projects are being pursued to define novel RGS domain-independent functions of RGS9-2 and to define the receptor- and pathway-specificity of RGS9-2 function.
A second major area of interest is to define the role of RGS proteins in the development and progression of Ovarian Cancer. G-protein activation by receptors is a well-studied factor in ovarian cancer pathology, but the role of counter-regulation of G-proteins by RGS proteins is largely unknown. Projects seek to characterize RGS expression in normal and cancerous ovarian tissue, and delineate the role of these RGS proteins in the regulation of cancer-related phenotypes such as growth, migration, and apoptosis.
Diverse biochemical and cellular techniques are used to address these biological questions:
• General molecular approaches: PCR, molecular biology, SDS-PAGE protein gels, immunoblotting, cell culture, transfection.
• Cell signaling studies: second messenger assays (IP3 and cAMP), immunoprecipitation and siRNA.
• Protein biochemistry: Protein purification, proteoliposome reconstitution, radioligand binding, enzyme kinetics.
- Representative Publications
- Jones, M., Siderovski, D., Hooks, S.B. (2004). GGL-ing at convention: Novelty and selectivity in the Gβ dimer. Molecular Interventions. 4: 200-214.
Hooks, S.B., Waldo, G.L., Corbitt, J., Bodor, E.T., Krumins, A.M., and Harden, T.K. (2003). RGS6, RGS7, RGS9 and RGS11 Stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity. Journal of Biological Chemistry. 278:10087-10093.
Wu, Y.-L., Hooks, S.B., Harden, T.K., Dohlman, H. (2004). Dominant-negative inhibition of pheromone receptor signaling by a single point mutation in the G protein subunit. Journal of Biological Chemistry. 279: 35287-97.
Hooks, S.B., Santos, W.L., Im, D.S., Macdonald, T.L., and Lynch, K.R. (2000). Lysophosphatidic Acid induced mitogenesis is regulated by Lipid Phosphate Phosphatases and is Edg-receptor independent. Journal of Biological Chemistry. 276:4611-4621.
Hooks, S.B., Ragan, S.P., Hopper, D.W., Honneman, C.W., Durieux, M.E., Macdonald, T.L., and Lynch, K.R. (1998). Characterization of a receptor subtype-selective lysophosphatidic acid mimetic. Molecular Pharmacology. 53: 188-194.