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The molecular and biochemical characterization of serine/threonine
protein kinase pathways that function in stress-related signal transduction
pathways.
Research Activities
The regulation of serine/threonine protein kinase pathways is
the research focus in my laboratory. These protein kinase pathways
are activated by a number of extracellular molecules. To study
these signal transduction pathways, molecular and biochemical
approaches will be utilized in order to understand the regulatory
mechanisms that affect the activity of these kinases. These intracellular
serine/threonine protein kinase pathways, which are referred to
as mitogen-activated protein (MAP) kinase pathways, are activated
by a number of hormones, growth factors, cytokines, and environmental
agents. Currently, at least four MAP kinase pathways have been
identified, and there are many protein kinases that function within
a defined MAP pathway, where each kinase phosphorylates and activates
a downstream kinase. One role for these sequential kinase pathways
is to transmit an extracellular signal from the plasma membrane
to the nucleus.
The cytoplasmic kinases that transmit the signal from the plasma
membrane to various MAP kinase proteins have not been characterized.
These kinases include the MAP/Extracellular signal-regulated kinase
(ERK) Kinase Kinase (MEKK) proteins. To date, at least four MEKK
proteins have been identified based on a homology to similar protein
kinases found in the budding yeast, Saccharomyces cerevisiae.
However, the extracellular molecules that regulate the MEKK proteins
remain largely undefined in mammalian cells. Since the MEKK proteins
participate as part of sequential MAP kinase pathways in mammalian
cells, it is hypothesized that these proteins are involved in
mediating some of the biological responses that cells use to proliferate,
differentiate, adapt, and survive. A major focus in my laboratory
is to characterize the role of MEKK proteins in cellular signal
transduction pathways.
Publications
(Query PubMed fot this investigator)
Adams, D.G., Sachs, N.A. and Vaillancourt, R.R. (2002). Phosphorylation
of the stress-activated protein kinase, MEKK3, at serine 166.
Arch. Biochem. Biophys.. (in press).
Tran, N.L., Adams, D.G., Vaillancourt, R.R. and Heimark, R.L.
(2002). Signaling from N-cadherin increases Bcl-2: regulation
of the phosphatidylinositol 3-kinase/Akt pathway via association
with the actin cytoskeleton. J. Biol. Chem. (in press).
Shi, J., Feng, Y., Goulet, A.-C., Vaillancourt, R.R., Sachs,
N.A., Hershey, J.W. and Nelson, M.A. (2002). The cyclin dependent
kinase CDC2 family member PITSLRE p100 interacts with the p47
subunit of eukaryotic initiation factor 3 during apoptosis. J.
Biol. Chem. (accepted pending revisions).
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