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Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum

The voltage-dependent anion channel (VDAC) is a ubiquitous channel in the outer membrane of the mitochondrion with multiple roles in protein, metabolite and small molecule transport. In mammalian cells, VDAC protein, as part of a larger complex including the inositol triphosphate receptor, has been...

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Autores principales: Mallo, Natalia, Ovciarikova, Jana, Martins-Duarte, Erica S., Baehr, Stephan C., Biddau, Marco, Wilde, Mary-Louise, Uboldi, Alessandro D., Lemgruber, Leandro, Tonkin, Christopher J., Wideman, Jeremy G., Harding, Clare R., Sheiner, Lilach
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Company of Biologists Ltd 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8572010/
https://www.ncbi.nlm.nih.gov/pubmed/34523684
http://dx.doi.org/10.1242/jcs.255299
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author Mallo, Natalia
Ovciarikova, Jana
Martins-Duarte, Erica S.
Baehr, Stephan C.
Biddau, Marco
Wilde, Mary-Louise
Uboldi, Alessandro D.
Lemgruber, Leandro
Tonkin, Christopher J.
Wideman, Jeremy G.
Harding, Clare R.
Sheiner, Lilach
author_facet Mallo, Natalia
Ovciarikova, Jana
Martins-Duarte, Erica S.
Baehr, Stephan C.
Biddau, Marco
Wilde, Mary-Louise
Uboldi, Alessandro D.
Lemgruber, Leandro
Tonkin, Christopher J.
Wideman, Jeremy G.
Harding, Clare R.
Sheiner, Lilach
author_sort Mallo, Natalia
collection PubMed
description The voltage-dependent anion channel (VDAC) is a ubiquitous channel in the outer membrane of the mitochondrion with multiple roles in protein, metabolite and small molecule transport. In mammalian cells, VDAC protein, as part of a larger complex including the inositol triphosphate receptor, has been shown to have a role in mediating contacts between the mitochondria and endoplasmic reticulum (ER). We identify VDAC of the pathogenic apicomplexan Toxoplasma gondii and demonstrate its importance for parasite growth. We show that VDAC is involved in protein import and metabolite transfer to mitochondria. Further, depletion of VDAC resulted in significant morphological changes in the mitochondrion and ER, suggesting a role in mediating contacts between these organelles in T. gondii. This article has an associated First Person interview with the first author of the paper.
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spelling pubmed-85720102021-11-12 Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum Mallo, Natalia Ovciarikova, Jana Martins-Duarte, Erica S. Baehr, Stephan C. Biddau, Marco Wilde, Mary-Louise Uboldi, Alessandro D. Lemgruber, Leandro Tonkin, Christopher J. Wideman, Jeremy G. Harding, Clare R. Sheiner, Lilach J Cell Sci Research Article The voltage-dependent anion channel (VDAC) is a ubiquitous channel in the outer membrane of the mitochondrion with multiple roles in protein, metabolite and small molecule transport. In mammalian cells, VDAC protein, as part of a larger complex including the inositol triphosphate receptor, has been shown to have a role in mediating contacts between the mitochondria and endoplasmic reticulum (ER). We identify VDAC of the pathogenic apicomplexan Toxoplasma gondii and demonstrate its importance for parasite growth. We show that VDAC is involved in protein import and metabolite transfer to mitochondria. Further, depletion of VDAC resulted in significant morphological changes in the mitochondrion and ER, suggesting a role in mediating contacts between these organelles in T. gondii. This article has an associated First Person interview with the first author of the paper. The Company of Biologists Ltd 2021-10-20 /pmc/articles/PMC8572010/ /pubmed/34523684 http://dx.doi.org/10.1242/jcs.255299 Text en © 2021. 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
Mallo, Natalia
Ovciarikova, Jana
Martins-Duarte, Erica S.
Baehr, Stephan C.
Biddau, Marco
Wilde, Mary-Louise
Uboldi, Alessandro D.
Lemgruber, Leandro
Tonkin, Christopher J.
Wideman, Jeremy G.
Harding, Clare R.
Sheiner, Lilach
Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
title Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
title_full Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
title_fullStr Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
title_full_unstemmed Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
title_short Depletion of a Toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
title_sort depletion of a toxoplasma porin leads to defects in mitochondrial morphology and contacts with the endoplasmic reticulum
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8572010/
https://www.ncbi.nlm.nih.gov/pubmed/34523684
http://dx.doi.org/10.1242/jcs.255299
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