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Vol. 13, Issue 4, 1190-1202, April 2002
*European Molecular Biology Laboratory, 69012 Heidelberg, Germany;
§Université Montpellier II, CNRS UMR 5539, CC 107, 34095 Montpellier Cedex 05, France
Actin assembly on membrane surfaces is an elusive process in which
several phosphoinositides (PIPs) 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.,
2000b). Here, we provide several lines of evidence that both
preexisting and newly synthesized PI(4,5)P2, and probably PI(4)P, are essential for phagosomal actin assembly; only these PIPs
were routinely synthesized 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 fivefold 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
LBPs 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 LBPs 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, because 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 PIPs on the organelle membrane.
Corresponding author. E-mail address:
griffiths{at}embl-heidelberg.de.
Present address: Observatoire Oceanologique de
Banyuls, UMR CNRS 7628, Banyuls/Mer, France
These authors contributed equally to this study.
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