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A more recent version of this article appeared on May 1, 2003
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Submitted on August 5, 2002
Revised on January 1, 2003
Accepted on January 16, 2003
1 Departement des Maladies Infectieuses, CNRS UMR 8104, Institut Cochin, 22 rue Mechain, 75014 Paris, France
2 Laboratoire de Physiologie de la reproduction ESA 7080, CNRS/INRA, 75005 Paris, France
3 Laboratoire des venims, Institut Pasteur, 75015 Paris, France
4 Laboratoire de Signalisation Immuno-Parasitaire - URA CNRS 1960, Institut Pasteur, 75015 Paris, France
* Corresponding author. E-mail address: tardieux{at}cochin.inserm.fr.
Actin polymerization in Apicomplexa protozoa is central to parasite motility and host cell invasion. Toxofilin has been characterized as a protein that sequesters actin monomers and caps actin filaments in Toxoplasma gondii. Here, we show that Toxofilin properties in vivo as in vitro depend on its phosphorylation. We identify a novel parasitic type 2C phosphatase that binds the Toxofilin/G-actin complex and a casein kinase II-like activity in the cytosol, both of which modulate the phosphorylation status of Toxofilin serine53. The interplay of these two molecules controls Toxofilin binding of G-actin as well as actin dynamics in vivo. Such functional interactions should play a major role in actin sequestration, a central feature of actin dynamics in Apicomplexa that underlies the spectacular speed and nature of parasite gliding motility.
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