Brian E. Wadzinski, Ph.D.
Associate Professor of Pharmacology
- : email@example.com
- : (615) 343-2080
406 Robinson Research Building
2220 Pierce Avenue
Nashville, Tennessee - 37232-6600
- : Brian E. Wadzinski, Ph.D. - CV
The integrated actions of both protein kinases and phosphatases govern the phosphorylation state of key intracellular proteins which are crucial for normal cellular function. Although less attention has been given to the protein serine/threonine phosphatases than to the serine/threonine kinases, it is nonetheless clear that this group of proteins plays an integral role in the control of cell growth and differentiation. Our overall research program is the study of cellular protein serine/threonine phosphatases (PPs); however, our studies have focused on PP2A-like enzymes. This family of holoenzymes has been implicated in many facets of cellular function including regulation of metabolic enzymes, cell-surface receptors, cytosolic protein kinases, and transcription factors. Moreover, PP2A itself is regulated in many ways which include association with regulatory subunits, activation or inactivation by associated proteins, and post-translational modifications. We are using multiple complementary approaches including biochemical, immunological, and molecular biology techniques to determine the structure, function, cellular localization, and regulation of PP2A-like enzymes. Particular emphasis has been placed on studying PP2A multi-protein complexes as a first step towards understanding in molecular detail the way phosphorylation/dephosphorylation reactions control cell signalling pathways. Our studies have revealed the existence of protein kinase/PP2A signaling modules as a new paradigm for the control of various intracellular signaling cascades.
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