Abstract
PTEN, a phosphatase that dephosphorylates the 3′ position of phosphoinositides, is a tumor suppressor. Activation of PTEN by PI-4,5-P2 requires a polybasic region at the N-terminus. It was hypothesized that PI-4,5-P2 aids membrane recruiting and induces a conformational change in PTEN. To test this hypothesis we have investigated the interaction of PTEN and a truncated PTEN lacking the N-terminal polybasic region with PI-4,5-P2/POPC mixed vesicles by infrared spectroscopy. PI-4,5-P2induces a conformational change in PTEN towards more α-helical content, but not for the truncated PTEN. The structural changes induced for PI-4,5-P2 were greater than those for other anionic lipids, e.g., PS and PI-4P. To further explore this conformational change, we have investigated the interaction of various peptides derived from the N-terminus of PTEN with different phosphoinositides. It was found by fluorescence quenching experiments of mixed POPC/Bodipy PI-4,5-P2 vesicles that PTEN1–16 induces PI-4,5-P2 domain formation....
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