Unconventional endosome-like compartment ...
Document type :
Compte-rendu et recension critique d'ouvrage
DOI :
Title :
Unconventional endosome-like compartment and retromer complex in Toxoplasma gondii govern parasite integrity and host infection
Author(s) :
Sangaré, Lamba Omar [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Dilezitoko Alayi, Tchilabalo [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Protéomique et Peptides Modifiés - PLBS [P3M]
Westermann, Benoit [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Hovasse, Agnes [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Sindikubwabo, Fabien [Auteur]
Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) [IAB]
Callebaut, Isabelle [Auteur]
Institut de minéralogie, de physique des matériaux et de cosmochimie [IMPMC]
Werkmeister, Elisabeth [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Lafont, Frank [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Slomianny, Christian [Auteur]
Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Hakimi, Mohamed-Ali [Auteur]
Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) [IAB]
van Dorsselaer, Alain [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Schaeffer-Reiss, Christine [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Tomavo, Stanislas [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Protéomique et Peptides Modifiés - PLBS [P3M]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Dilezitoko Alayi, Tchilabalo [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Protéomique et Peptides Modifiés - PLBS [P3M]
Westermann, Benoit [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Hovasse, Agnes [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Sindikubwabo, Fabien [Auteur]
Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) [IAB]
Callebaut, Isabelle [Auteur]
Institut de minéralogie, de physique des matériaux et de cosmochimie [IMPMC]
Werkmeister, Elisabeth [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Lafont, Frank [Auteur]
Institut de biologie de Lille - UMS 3702 [IBL]
Slomianny, Christian [Auteur]
Laboratoire de Physiologie Cellulaire - U 1003 [PHYCELL]
Hakimi, Mohamed-Ali [Auteur]
Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) [IAB]
van Dorsselaer, Alain [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Schaeffer-Reiss, Christine [Auteur]
Institut Pluridisciplinaire Hubert Curien [IPHC]
Tomavo, Stanislas [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]
Protéomique et Peptides Modifiés - PLBS [P3M]
Journal title :
Nature Communications
Pages :
11191
Publisher :
Nature Publishing Group
Publication date :
2016-04
ISSN :
2041-1723
HAL domain(s) :
Sciences du Vivant [q-bio]
English abstract : [en]
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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Popular science :
Non
ANR Project :
Source :
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