Contacting domains segregate a lipid transporter from a solute transporter in the malarial host–parasite interface
| العنوان: | Contacting domains segregate a lipid transporter from a solute transporter in the malarial host–parasite interface |
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| المؤلفون: | Tatyana Tenkova-Heuser, Christopher K. E. Bleck, John E. Heuser, Daniel E. Goldberg, Eva S. Istvan, Joshua Zimmerberg, Robyn Roth, Matthias Garten, Josh R. Beck |
| المصدر: | Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020) Nature Communications |
| بيانات النشر: | Nature Publishing Group, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | 0301 basic medicine, Cytoplasm, Erythrocytes, Science, Plasmodium falciparum, Protozoan Proteins, General Physics and Astronomy, Membrane trafficking, General Biochemistry, Genetics and Molecular Biology, Article, Host-Parasite Interactions, 03 medical and health sciences, 0302 clinical medicine, Organelle, parasitic diseases, Extracellular, Parasite hosting, Humans, Malaria, Falciparum, lcsh:Science, Multidisciplinary, Chemistry, Intracellular parasite, Cell Membrane, Membrane Transport Proteins, Transporter, Biological Transport, Membrane structure and assembly, General Chemistry, Intracellular Membranes, Lipids, Transport protein, Cell biology, Parasite biology, Protein Transport, 030104 developmental biology, Membrane, Vacuoles, lcsh:Q, 030217 neurology & neurosurgery |
| الوصف: | The malaria parasite interfaces with its host erythrocyte (RBC) using a unique organelle, the parasitophorous vacuole (PV). The mechanism(s) are obscure by which its limiting membrane, the parasitophorous vacuolar membrane (PVM), collaborates with the parasite plasma membrane (PPM) to support the transport of proteins, lipids, nutrients, and metabolites between the cytoplasm of the parasite and the cytoplasm of the RBC. Here, we demonstrate that the PV has structure characterized by micrometer-sized regions of especially close apposition between the PVM and the PPM. To determine if these contact sites are involved in any sort of transport, we localize the PVM nutrient-permeable and protein export channel EXP2, as well as the PPM lipid transporter PfNCR1. We find that EXP2 is excluded from, but PfNCR1 is included within these regions of close apposition. We conclude that the host-parasite interface is structured to segregate those transporters of hydrophilic and hydrophobic substrates. While membrane contact sites between intracellular organelles are abundant, little is known about the contacts between membranes that delimit extracellular junctions within cells, such as intracellular parasites. Here authors demonstrate the segregation of a lipid transporter from a solute transporter in the malarial host-parasite interface. |
| اللغة: | English |
| تدمد: | 2041-1723 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb28e11bc95cf1d715229ce1c1672b0d http://link.springer.com/article/10.1038/s41467-020-17506-9 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....bb28e11bc95cf1d715229ce1c1672b0d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 20411723 |
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