Dipti Bhoiwala (2005)

Albany Medical College

Adapt78 is a novel stress-inducible and cytoprotective gene in mammalian cells. The gene produces a protein that binds to and inhibits intracellular calcineurin, a phosphatase that mediates many cellular responses to calcium. Calcineurin is involved in many cellular and
tissue functions, and its abnormal expression is associated with multiple pathologies. I have investigated the mechanism of action of Adapt78 in response to calcium and oxidative stress, by
characterizing cell receptor-based signaling pathways that lead to Adapt78 induction. These studies have been carried out on several different cell types stimulating receptors known to cause a calcium and reactive oxygen species release to induce Adapt78.
These analyses will thus allow me to test the hypothesis that Adapt78 is an important regulator of cell receptor signaling. These studies have indicated that
physiologically-relevant cell receptor signaling can lead to the induction of Adapt78, suggesting the importance of Adapt78 in signal transduction. Adpat78 is implicated in diseases such as Down’s syndrome and Alzheimer’s.

Bradley DeMay (2005)

Dartmouth University

I'm trying to rescue a phenotype of Arabidopsis, trying to put a gene back into a knockout. The gene is ARR12 and functions in phosphorylation cascades in cytokinin signaling. I'm reconstructing the gene using the genomic DNA for the promoter and cDNA for the actual gene. I had to design primers and amplify the DNA while adding restriction enzyme sites and then insert it into our plasmid. Then I'll have two plasmids, one with the promoter and one with gene. I'll cut out the gene and paste it in with the promoter so that I'll have one large construct. Then I'll switch it over to a plasmid that has the ability to insert its DNA into plants and hopefully grow up a fully functional Arabidopsis plant.

Stephanie Guzik (2005)

NIH/University of North Carolina-Chapel Hill

My first rotation was at NIH in Bethesda, MD where I worked with Dr. James Sellers investigating the movements of two actin-associated motor proteins, Myosin II and Myosin V. The work was primarily focused on biophysical and biochemical aspects of actin bundling with fibrin and the subsequent movement of the myosins on these actin bundles. More recently, I've been rotating in the lab of Dr. Keith Burridge at UNC where I've been studying the regulation of Rho-GEF proteins. My work has focused on cell biology and protein-binding interactions between GEFs and potential regulators. Finally, I'll be rotating in the lab of Dr. Carol Otey, also at UNC, examining the activities of astrocyte cells in primary culture to mimick the events involved in the formation of a glial scar, which is generated in the brain following injury.

Rebecca Lock (2005)

University of California, San Francisco

The project that I'm working on first in my first rotation involves trying to locate a certain protein equivalent in Dictyostelium. Dictyostelium is an amoeba slime mold organism that people use a lot in chemotaxis assays since it has a very defined chemotaxis response.