IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii
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 mitocho...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists Ltd
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9845740/ https://www.ncbi.nlm.nih.gov/pubmed/36314270 http://dx.doi.org/10.1242/jcs.260083 |
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author | Oliveira Souza, Rodolpho Ornitz Jacobs, Kylie N. Back, Peter S. Bradley, Peter J. Arrizabalaga, Gustavo |
author_facet | Oliveira Souza, Rodolpho Ornitz Jacobs, Kylie N. Back, Peter S. Bradley, Peter J. Arrizabalaga, Gustavo |
author_sort | Oliveira Souza, Rodolpho Ornitz |
collection | PubMed |
description | 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-shaped mitochondrion. 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. This article has an associated First Person interview with the first author of the paper. |
format | Online Article Text |
id | pubmed-9845740 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Company of Biologists Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-98457402023-02-06 IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii Oliveira Souza, Rodolpho Ornitz Jacobs, Kylie N. Back, Peter S. Bradley, Peter J. Arrizabalaga, Gustavo J Cell Sci Research Article 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-shaped mitochondrion. 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. This article has an associated First Person interview with the first author of the paper. The Company of Biologists Ltd 2022-11-15 /pmc/articles/PMC9845740/ /pubmed/36314270 http://dx.doi.org/10.1242/jcs.260083 Text en © 2022. Published by The Company of Biologists Ltd https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Oliveira Souza, Rodolpho Ornitz Jacobs, Kylie N. Back, Peter S. Bradley, Peter J. Arrizabalaga, Gustavo IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii |
title | IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii |
title_full | IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii |
title_fullStr | IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii |
title_full_unstemmed | IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii |
title_short | IMC10 and LMF1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in Toxoplasma gondii |
title_sort | imc10 and lmf1 mediate mitochondrial morphology through mitochondrion–pellicle contact sites in toxoplasma gondii |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9845740/ https://www.ncbi.nlm.nih.gov/pubmed/36314270 http://dx.doi.org/10.1242/jcs.260083 |
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