Abstract
PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a tumor suppressor protein that dephosphorylates phosphoinositides at the 3-position of the inositol ring. PTEN's membrane association has been shown to be a complex process that involves binding to phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] and phosphatidylserine [PS]. Recent evidence suggests that the presence of cholesterol promotes the formation of PI(4,5)P2 enriched domains. This study has three objectives: First, to investigate PTEN's binding to lipid systems with laterally heterogeneous membrane morphology. Second, to delineate the kinetics of PTEN lipid binding and activation using stopped-flow fluorescence measurements. Third, by using single molecule fluorescence microscopy determine the lateral diffusion of membrane bound PTEN on supported bilayer and how the binding is affected by laterally heterogeneous membrane environments. Overall the study aims to understand the dynamics of PTEN-membrane interactions at the molecular level.
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