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Originally published as MBC in Press, 10.1091/mbc.E02-08-0462 on February 6, 2003

Vol. 14, Issue 5, 1900-1912, May 2003

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Actin Dynamics Is Controlled by a Casein Kinase II and Phosphatase 2C Interplay on Toxoplasma gondii Toxofilin

Violaine Delorme *, Xavier Cayla {dagger}, Grazyna Faure {ddagger}, Alphonse Garcia §, and Isabelle Tardieux * ||

* Departement des Maladies Infectieuses, Centre National de la Recherche Scientifique Unité Mixte Recherche 8104, Institut Cochin, 75014 Paris, France; {dagger} Laboratoire de Physiologie de la reproduction ESA 7080, Centre National de la Recherche Scientifique/Institut National de la Recherche Agronomique, 75005 Paris, France; {ddagger} Laboratoire des venims, Institut Pasteur, 75015 Paris, France; and § Laboratoire de Signalisation Immuno-Parasitaire, Unité de Recherche Associée Centre National de la Recherche Scientifique 1960, Institut Pasteur, 75015 Paris, France

Submitted August 5, 2002; Revised January 10, 2003; Accepted January 16, 2003
Monitoring Editor: David Drubin

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. Herein, 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.

Article published online ahead of print. Mol. Biol. Cell 10.1091/mbc.E02-08-0462. Article and publication date are at www.molbiolcell.org/cgi/doi/10.1091/mbc.E02-08-0462.

Corresponding author. E-mail address: tardieux{at}cochin.inserm.fr.




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