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First published online 30 November 2004
doi: 10.1242/jcs.01579

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In vivo analysis of 3-phosphoinositide dynamics during Dictyostelium phagocytosis and chemotaxis

¹ Division of Cell and Developmental Biology, MSI/WTB Complex, University of Dundee, Dow Street, Dundee, DD1 5EH, UK
² BioFocus Limited, Milton Road, Cambridge, CB4 0FG, UK

^* Author for correspondence (e-mail: c.j.weijer{at}dundee.ac.uk)

Accepted 5 October 2004

Phagocytosis and chemotaxis are receptor-mediated processes that require extensive rearrangements of the actin cytoskeleton, and are controlled by lipid second messengers such as phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P₃] and phosphatidylinositol 3,4-bisphosphate [PtdIns(3,4)P₂]. We used a panel of pleckstrin homology (PH) domains with distinct binding specificities for PtdIns(3,4,5)P₃ and PtdIns(3,4)P₂ to study the spatiotemporal dynamics of these phosphoinositides in vivo. During phagocytosis and macropinocytosis PtdIns(3,4,5)P₃ levels transiently increased at sites of engulfment, followed by a rapid PtdIns(3,4)P₂ production round the phagosome/macropinosome upon its internalisation, suggesting that PtdIns(3,4,5)P₃ is degraded to PtdIns(3,4)P₂. PTEN null mutants, which are defective in phagocytosis, showed normal rates of PtdIns(3,4,5)P₃degradation, but unexpectedly an accelerated PtdIns(3,4)P₂ degradation. During chemotaxis to cAMP only PtdIns(3,4,5)P₃ was formed in the plasma membrane, and no PtdIns(3,4)P₂ was detectable, showing that all PtdIns(3,4,5)P₃ was degraded by PTEN to PtdIns(4,5)P₂. Furthermore, we showed that different PtdIns(3,4,5)P₃ binding PH domains gave distinct spatial and temporal readouts of the same underlying PtdIns(3,4,5)P₃ signal, enabling distinct biological responses to one signal.

Key words: Phagocytosis, Chemotaxis, Phosphoinositide, PH domain, Imaging

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