التفاصيل البيبلوغرافية
| العنوان: |
IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion--pellicle contact sites in Toxoplasma gondii. |
| المؤلفون: |
Oliveira Souza, Rodolpho Ornitz, Jacobs, Kylie N., Back, Peter S., Bradley, Peter J., Arrizabalaga, Gustavo |
| المصدر: |
Journal of Cell Science; Nov2022, Vol. 135 Issue 22, p1-15, 15p |
| مصطلحات موضوعية: |
TOXOPLASMA gondii, MITOCHONDRIA, MITOCHONDRIAL membranes, INTRACELLULAR pathogens, MITOCHONDRIAL proteins, MORPHOLOGY, PLANT mitochondria |
| مستخلص: |
The single mitochondrion of Toxoplasma gondii is highly dynamic, being predominantly in a peripherally distributed lasso-shape in intracellular parasites and collapsed in extracellular parasites. The peripheral positioning of the mitochondrion is associated with apparent contacts between the mitochondrion membrane and the parasite pellicle. The outer mitochondrial membrane-associated protein LMF1 is critical for the correct positioning of the mitochondrion. Intracellular parasites lacking LMF1 fail to form the lasso-shapedmitochondrion. To identify other proteins that tether the mitochondrion of the parasite to the pellicle, we performed a yeast two-hybrid screen for LMF1 interactors. We identified 70 putative interactors localized in different cellular compartments, such as the apical end of the parasite, mitochondrial membrane and the inner membrane complex (IMC), including with the pellicle protein IMC10. Using protein--protein interaction assays, we confirmed the interaction of LMF1 with IMC10. Conditional knockdown of IMC10 does not affect parasite viability but severely affects mitochondrial morphology in intracellular parasites and mitochondrial distribution to the daughter cells during division. In effect, IMC10 knockdown phenocopies disruption of LMF1, suggesting that these two proteins define a novel membrane tether between the mitochondrion and the IMC in Toxoplasma. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
Complementary Index |
