scholarly journals Structure of Toxoplasma gondii coronin, an actin‐binding protein that relocalizes to the posterior pole of invasive parasites and contributes to invasion and egress

2014 ◽  
Vol 28 (11) ◽  
pp. 4729-4747 ◽  
Author(s):  
Julien Salamun ◽  
Juha P. Kallio ◽  
Wassim Daher ◽  
Dominique Soldati‐Favre ◽  
Inari Kursula
Keyword(s):  
Toxoplasma Gondii ◽  
Binding Protein ◽  
Posterior Pole ◽  
Actin Binding ◽  
Actin Binding Protein

scholarly journals The actin-binding protein Lasp promotes Oskar accumulation at the posterior pole of the Drosophila embryo

Development ◽  
2008 ◽  
Vol 136 (1) ◽  
pp. 95-105 ◽  
Author(s):  
R. Suyama ◽  
A. Jenny ◽  
S. Curado ◽  
W. Pellis-van Berkel ◽  
A. Ephrussi
Keyword(s):  
Binding Protein ◽  
Posterior Pole ◽  
Drosophila Embryo ◽  
Actin Binding ◽  
Actin Binding Protein

scholarly journals Toxofilin, a Novel Actin-binding Protein from Toxoplasma gondii, Sequesters Actin Monomers and Caps Actin Filaments

2000 ◽  
Vol 11 (1) ◽  
pp. 355-368 ◽  
Author(s):  
Olivier Poupel ◽  
Haralabia Boleti ◽  
Sophie Axisa ◽  
Evelyne Couture-Tosi ◽  
Isabelle Tardieux
Keyword(s):  
Green Fluorescent Protein ◽  
Toxoplasma Gondii ◽  
Host Cell ◽  
Actin Filaments ◽  
Actin Polymerization ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Actin Binding ◽  
Actin Binding Protein ◽  
Green Fluorescent

Toxoplasma gondii relies on its actin cytoskeleton to glide and enter its host cell. However, T. gondii tachyzoites are known to display a strikingly low amount of actin filaments, which suggests that sequestration of actin monomers could play a key role in parasite actin dynamics. We isolated a 27-kDa tachyzoite protein on the basis of its ability to bind muscle G-actin and demonstrated that it interacts with parasite G-actin. Cloning and sequence analysis of the gene coding for this protein, which we named Toxofilin, showed that it is a novel actin-binding protein. In in vitro assays, Toxofilin not only bound to G-actin and inhibited actin polymerization as an actin-sequestering protein but also slowed down F-actin disassembly through a filament end capping activity. In addition, when green fluorescent protein-tagged Toxofilin was overexpressed in mammalian nonmuscle cells, the dynamics of actin stress fibers was drastically impaired, whereas green fluorescent protein-Toxofilin copurified with G-actin. Finally, in motile parasites, during gliding or host cell entry, Toxofilin was localized in the entire cytoplasm, including the rear end of the parasite, whereas in intracellular tachyzoites, especially before they exit from the parasitophorous vacuole of their host cell, Toxofilin was found to be restricted to the apical end.

Clathrin Hub Expression Dissociates the Actin-Binding Protein Hip1R from Coated Pits and Disrupts Their Alignment with the Actin Cytoskeleton

Traffic ◽  
2001 ◽  
Vol 2 (11) ◽  
pp. 851-858 ◽  
Author(s):  
Elizabeth M. Bennett ◽  
Chih-Ying Chen ◽  
Asa E. Y. Engqvist-Goldstein ◽  
David G. Drubin ◽  
Frances M. Brodsky
Keyword(s):  
Actin Cytoskeleton ◽  
Binding Protein ◽  
Actin Binding ◽  
Coated Pits ◽  
Actin Binding Protein

Binding of Human Platelet Glycoprotein lb and Actin to Fragments of Actin-Binding Protein

1992 ◽  
Vol 67 (02) ◽  
pp. 252-257 ◽  
Author(s):  
Anne M Aakhus ◽  
J Michael Wilkinson ◽  
Nils Olav Solum
Keyword(s):  
Actin Filaments ◽  
High Speed ◽  
Binding Protein ◽  
Protein A ◽  
Actin Binding ◽  
Platelet Glycoprotein ◽  
Actin Binding Protein ◽  
Crossed Immunoelectrophoresis ◽  
Triton X ◽  
Calpain Inhibitors

SummaryActin-binding protein (ABP) is degraded into fragments of 190 and 90 kDa by calpain. A monoclonal antibody (MAb TI10) against the 90 kDa fragment of ABP coprecipitated with the glycoprotein lb (GP lb) peak observed on crossed immunoelectrophoresis of Triton X-100 extracts of platelets prepared without calpain inhibitors. MAb PM6/317 against the 190 kDa fragment was not coprecipitated with the GP lb peak under such conditions. The 90 kDa fragment was adsorbed on protein A agarose from extracts that had been preincubated with antibodies to GP lb. This supports the idea that the GP Ib-ABP interaction resides in the 90 kDa region of ABP. GP lb was sedimented with the Triton-insoluble actin filaments in trace amounts only, and only after high speed centrifugation (100,000 × g, 3 h). Both the 190 kDa and the 90 kDa fragments of ABP were sedimented with the Triton-insoluble actin filaments.

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