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Published Papers
Our lab is interested in understanding the molecular processes that underlie the genesis and progression of human tumors. Our current and future work is directed towards the following three interconnected areas: 1) the functional characterization of physiologic and cancer-related post translational regulation of PP2A, 2) identifying the biological and structural basis for the evolutionary selection and fitness of cancer-derived mutations of PP2A and, 3) the development and characterization of small molecule
Protein phosphatases are vital molecular switches that balance many cellular processes through the reversible de-phosphorylation of key signaling proteins. Protein Phosphatase 2A (PP2A) is a serine/threonine phosphatase that regulates many oncogenic signaling pathways, thereby biologically functioning as a tumor suppressor. The structure of PP2A is a trimeric holoenzyme composed of a catalytic subunit C, a scaffolding subunit A, and one of many different regulatory subunits B, which dictate PP2A substrate s