| Glover,
Claiborne V. C. |
E-mail:
glover@uga.edu |
| Dr. Glover's group
is involved in the study of protein phosphorylation as a regulatory
mechanism in eukaryotic cells. His group is currently focusing
on casein kinase II (CKII), a ubiquitous and highly conserved
Ser/Thr protein kinase that phosphorylates a broad spectrum
of nuclear and cytoplasmic substrates. The physiological role
of CKII is being explored using the budding yeast Saccharomyces
cerevisiae as a model system. Biochemical, molecular, genetic,
and genomics approaches are employed. |
| Keywords: protein kinase,
casein kinase II, cell cycle, cell polarity, genomics, proteomics |
|
| Puett,
J. David |
E-mail:
puett@bmb.uga.edu |
| Dr. Puett's laboratory
is engaged in research on glycoprotein hormones and their cognate
G protein-coupled receptors, with emphasis on molecular and
cellular reproductive biochemical endocrinology and tumor biology.
One of the major goals being addressed is that of the molecular
mechanism of ligand-mediated receptor activation necessary for
intracellular signaling. Techniques employed include protein
engineering, site-directed mutagenesis, protein expression,
cell culture, determination of signaling pathways, characterization
of tumor antigens, and transgenic mice. Using ethnobotanical
information, research is also conducted on natural products
extracted from plants and assayed via high-throughput screening. |
| Keywords: glycoprotein
hormones, G protein-coupled receptors, transgenic mice, cancer,
natural products |
|
| Schmidt,
Walter K. |
E-mail:
wschmidt@bmb.uga.edu |
| Research in our
lab is focused on three proteases: Rce1, Ste24 and Axl1. These
membrane-localized proteases, two of which are zinc-dependent
enzymes, are required for the biogenesis of certain prenylated
signaling molecules. Prenylated proteins contain a covalently
attached lipid at the C-terminus and are exemplified by Ras,
Ras-related proteins, and secreted fungal mating pheromones.
Because prenylated molecules function in a variety of cellular
pathways that are linked to human disease (e.g. Ras and cancer),
understanding the roles of Rce1, Ste24 and Axl1 in the biogenesis
of prenylated molecules may lead to novel therapeutic strategies
for cancer and other diseases. |
| Keywords: cancer, protease,
post-translational modifications, prenylation, signaling, yeast |
|
| Wells, Lance |
E-mail: lwells@ccrc.uga.edu |
| Our broad research interest is in understanding how post-translational modifications modulate the properties of proteins. Specifically, we study "nutrient sensing" by characterizing the enzymes responsible for post-translational modification of proteins that have been implicated in responding to nutrients and regulating signal transduction cascades. Our lab uses a combination of methodologies including mass spectrometry, protein biochemistry, cell biology, proteomics, and molecular biology. We perform our experiments in vitro, in mammalian cell culture systems, and in the model organism C. elegans. We are currently focusing on the regulatory role of glycosylation in the development of type II diabetes, cancer, and congenital muscular dystrophy. |
| Keywords: glycosylation, phosphorylation, mass spectrometry, proteomics, signal transduction, diabetes, cancer, protein biochemistry |
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