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A more recent version of this article appeared on April 1, 2002
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Submitted on June 26, 2001
Revised on December 21, 2001
Accepted on January 14, 2002
1 European Molecular Biology Laboratory, Heidelberg, Germany (present address: Observatoire Oceanologique de Banyuls, UMR CNRS 7628, Banyuls/Mer, France)
2 European Molecular Biology Laboratory, Heidelberg, Germany
3 Université Montpellier II, CNRS UMR 5539, CC 107, 34095 Montpellier Cedex 05, France
4 European Molecular Biology Laboratory, Meyerhoffstrasse 1, Postfach 102209, 69012 Heidelberg, Germany
* Corresponding author. E-mail address: griffiths{at}embl-heidelberg.de.
Actin assembly on membrane surfaces is an elusive process in which several phosphoinositides (PIP's) have been implicated. We have reconstituted actin assembly using a defined membrane surface, the latex bead phagosome (LBP), and shown that the PI(4,5)P2-binding proteins ezrin and/or moesin were essential for this process (Defacque et al., EMBO J. 19:199-212, 2000). Here, we provide several lines of evidence that both pre-existing and newly synthesised PI(4,5)P2, and likely PI(4)P, are essential for phagosomal actin assembly; only these PIP's were routinely synthesised from ATP during in vitro actin assembly. Treatment of LBP with phospholipase C or with adenosine, an inhibitor of type II PI 4-kinase? as well as preincubation with anti-PI(4)P or anti-PI(4,5)P2 antibodies all inhibited this process. Incorporation of extra PI(4)P or PI(4,5)P2 into the LBP membrane led to a five-fold increase in the number of phagosomes that assemble actin. An ezrin mutant mutated in the PI(4,5)P2-binding sites was less efficient in binding to LBP, and in reconstituting actin assembly than wild-type ezrin. Our data show that PI 4- and PI 5-kinase, and under some conditions also PI 3-kinase activities are present on LBP and can be activated by ATP, even in the absence of GTP or cytosolic components. However, PI 3-kinase activity is not required for actin assembly since the process was not affected by PI 3-kinase inhibitors. We suggest that the ezrin-dependent actin assembly on the LBP membrane may require active turnover of D4 and D5 PIP's on the organelle membrane.
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