Fiche publication
Date publication
avril 2016
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Mme SCHAEFFER-REISS Christine
,
Dr VAN DORSSELAER Alain
Tous les auteurs :
Sangaré LO, Alayi TD, Westermann B, Hovasse A, Sindikubwabo F, Callebaut I, Werkmeister E, Lafont F, Slomianny C, Hakimi MA, Van Dorsselaer A, Schaeffer-Reiss C, Tomavo S
Lien Pubmed
Résumé
Membrane trafficking pathways play critical roles in Apicomplexa, a phylum of protozoan parasites that cause life-threatening diseases worldwide. Here we report the first retromer-trafficking interactome in Toxoplasma gondii. This retromer complex includes a trimer Vps35-Vps26-Vps29 core complex that serves as a hub for the endosome-like compartment and parasite-specific proteins. Conditional ablation of TgVps35 reveals that the retromer complex is crucial for the biogenesis of secretory organelles and for maintaining parasite morphology. We identify TgHP12 as a parasite-specific and retromer-associated protein with functions unrelated to secretory organelle formation. Furthermore, the major facilitator superfamily homologue named TgHP03, which is a multiple spanning and ligand transmembrane transporter, is maintained at the parasite membrane by retromer-mediated endocytic recycling. Thus, our findings highlight that both evolutionarily conserved and unconventional proteins act in concert in T. gondii by controlling retrograde transport that is essential for parasite integrity and host infection.
Mots clés
Amino Acid Sequence, Animals, Cell Compartmentation, Cell Membrane, metabolism, Endocytosis, Endosomes, metabolism, Gene Silencing, Genes, Protozoan, Host-Parasite Interactions, Molecular Sequence Data, Multiprotein Complexes, metabolism, Organelle Biogenesis, Parasites, metabolism, Phenotype, Protein Interaction Mapping, Protozoan Proteins, chemistry, Species Specificity, Toxoplasma, genetics, Vesicular Transport Proteins, metabolism
Référence
Nat Commun. 2016 Apr;7:11191
