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© Research
Publication : Molecular biology of the cell

Actin dynamics is controlled by a casein kinase II and phosphatase 2C interplay on Toxoplasma gondii Toxofilin

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular biology of the cell - 06 Feb 2003

Delorme V, Cayla X, Faure G, Garcia A, Tardieux I

Link to Pubmed [PMID] – 12802063

Mol. Biol. Cell 2003 May;14(5):1900-12

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.

https://www.ncbi.nlm.nih.gov/pubmed/12802063