| Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii. | |
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MedLine Citation:
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PMID: 20949068 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The invasive forms of apicomplexan parasites share a conserved form of gliding motility that powers parasite migration across biological barriers, host cell invasion and egress from infected cells. Previous studies have established that the duration and direction of gliding motility are determined by actin polymerization; however, regulators of actin dynamics in apicomplexans remain poorly characterized. In the absence of a complete ARP2/3 complex, the formin homology 2 domain containing proteins and the accessory protein profilin are presumed to orchestrate actin polymerization during host cell invasion. Here, we have undertaken the biochemical and functional characterization of two Toxoplasma gondii formins and established that they act in concert as actin nucleators during invasion. The importance of TgFRM1 for parasite motility has been assessed by conditional gene disruption. The contribution of each formin individually and jointly was revealed by an approach based upon the expression of dominant mutants with modified FH2 domains impaired in actin binding but still able to dimerize with their respective endogenous formin. These mutated FH2 domains were fused to the ligand-controlled destabilization domain (DD-FKBP) to achieve conditional expression. This strategy proved unique in identifying the non-redundant and critical roles of both formins in invasion. These findings provide new insights into how controlled actin polymerization drives the directional movement required for productive penetration of parasites into host cells. |
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Authors:
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Wassim Daher; Fabienne Plattner; Marie-France Carlier; Dominique Soldati-Favre |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-10-07 |
Journal Detail:
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Title: PLoS pathogens Volume: 6 ISSN: 1553-7374 ISO Abbreviation: PLoS Pathog. Publication Date: 2010 |
Date Detail:
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Created Date: 2010-10-15 Completed Date: 2011-03-07 Revised Date: 2011-08-31 |
Medline Journal Info:
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Nlm Unique ID: 101238921 Medline TA: PLoS Pathog Country: United States |
Other Details:
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Languages: eng Pagination: e1001132 Citation Subset: IM |
Affiliation:
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Department of Microbiology and Molecular Medicine, CMU, University of Geneva, Geneva, Switzerland. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actins
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metabolism Amino Acid Motifs / physiology Amino Acid Sequence Fetal Proteins / chemistry, genetics, metabolism, physiology Host-Parasite Interactions / physiology* Microfilament Proteins / chemistry, genetics, metabolism, physiology* Microscopy, Video Models, Biological Molecular Sequence Data Movement / physiology* Mutant Proteins / metabolism, physiology Nuclear Proteins / chemistry, genetics, metabolism, physiology Protein Multimerization / genetics Protein Structure, Tertiary / genetics Tissue Distribution Toxoplasma / genetics*, metabolism, physiology*, ultrastructure |
| Grant Support | |
ID/Acronym/Agency:
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//Howard Hughes Medical Institute |
| Chemical | |
Reg. No./Substance:
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0/Actins; 0/Fetal Proteins; 0/Microfilament Proteins; 0/Mutant Proteins; 0/Nuclear Proteins; 147336-47-8/formin 1 |
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