Design and Computational Modeling of a Chemically-Inducible Variant of the Protein Kinase, Akt1
Robert Newman, Ph.D.
Department of Biology
Protein phosphorylation, mediated by protein kinases, is one of the most widespread regulatory mechanisms in eukaryotes. Inside the cell, protein kinases, phosphatases, and their respective substrates are organized into integrated phosphorylation networks that govern nearly all aspects of cellular physiology. Likewise, dysregulation of these pathways leads to a variety of pervasive diseases, including cancer and diabetes. Unfortunately, due to the complexity of cellular phosphorylation networks, it has been difficult to dissect the functional roles of individual kinases within a given cellular network. Here, we describe the design, computational modeling and initial construction of a chemically-inducible variant of the canonical serine/ threonine protein kinase, AKT1. Successful construction of this new molecular tool will lead to a better understanding of the effect that AKT1 has on the cellular signaling system as a whole.
Peagler, Correggio, "Design and Computational Modeling of a Chemically-Inducible Variant of the Protein Kinase, Akt1" (2019). Undergraduate Research and Creative Inquiry Symposia. 92.