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A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria
To broadly explore mitochondrial structure and function as well as the communication of mitochondria with other cellular pathways, we constructed a quantitative, high-density genetic interaction map (the MITO-MAP) in Saccharomyces cerevisiae. The MITO-MAP provides a comprehensive view of mitochondri...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3198156/ https://www.ncbi.nlm.nih.gov/pubmed/21987634 http://dx.doi.org/10.1083/jcb.201107053 |
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author | Hoppins, Suzanne Collins, Sean R. Cassidy-Stone, Ann Hummel, Eric DeVay, Rachel M. Lackner, Laura L. Westermann, Benedikt Schuldiner, Maya Weissman, Jonathan S. Nunnari, Jodi |
author_facet | Hoppins, Suzanne Collins, Sean R. Cassidy-Stone, Ann Hummel, Eric DeVay, Rachel M. Lackner, Laura L. Westermann, Benedikt Schuldiner, Maya Weissman, Jonathan S. Nunnari, Jodi |
author_sort | Hoppins, Suzanne |
collection | PubMed |
description | To broadly explore mitochondrial structure and function as well as the communication of mitochondria with other cellular pathways, we constructed a quantitative, high-density genetic interaction map (the MITO-MAP) in Saccharomyces cerevisiae. The MITO-MAP provides a comprehensive view of mitochondrial function including insights into the activity of uncharacterized mitochondrial proteins and the functional connection between mitochondria and the ER. The MITO-MAP also reveals a large inner membrane–associated complex, which we term MitOS for mitochondrial organizing structure, comprised of Fcj1/Mitofilin, a conserved inner membrane protein, and five additional components. MitOS physically and functionally interacts with both outer and inner membrane components and localizes to extended structures that wrap around the inner membrane. We show that MitOS acts in concert with ATP synthase dimers to organize the inner membrane and promote normal mitochondrial morphology. We propose that MitOS acts as a conserved mitochondrial skeletal structure that differentiates regions of the inner membrane to establish the normal internal architecture of mitochondria. |
format | Online Article Text |
id | pubmed-3198156 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-31981562012-04-17 A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria Hoppins, Suzanne Collins, Sean R. Cassidy-Stone, Ann Hummel, Eric DeVay, Rachel M. Lackner, Laura L. Westermann, Benedikt Schuldiner, Maya Weissman, Jonathan S. Nunnari, Jodi J Cell Biol Research Articles To broadly explore mitochondrial structure and function as well as the communication of mitochondria with other cellular pathways, we constructed a quantitative, high-density genetic interaction map (the MITO-MAP) in Saccharomyces cerevisiae. The MITO-MAP provides a comprehensive view of mitochondrial function including insights into the activity of uncharacterized mitochondrial proteins and the functional connection between mitochondria and the ER. The MITO-MAP also reveals a large inner membrane–associated complex, which we term MitOS for mitochondrial organizing structure, comprised of Fcj1/Mitofilin, a conserved inner membrane protein, and five additional components. MitOS physically and functionally interacts with both outer and inner membrane components and localizes to extended structures that wrap around the inner membrane. We show that MitOS acts in concert with ATP synthase dimers to organize the inner membrane and promote normal mitochondrial morphology. We propose that MitOS acts as a conserved mitochondrial skeletal structure that differentiates regions of the inner membrane to establish the normal internal architecture of mitochondria. The Rockefeller University Press 2011-10-17 /pmc/articles/PMC3198156/ /pubmed/21987634 http://dx.doi.org/10.1083/jcb.201107053 Text en © 2011 Hoppins et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Hoppins, Suzanne Collins, Sean R. Cassidy-Stone, Ann Hummel, Eric DeVay, Rachel M. Lackner, Laura L. Westermann, Benedikt Schuldiner, Maya Weissman, Jonathan S. Nunnari, Jodi A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
title | A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
title_full | A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
title_fullStr | A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
title_full_unstemmed | A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
title_short | A mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
title_sort | mitochondrial-focused genetic interaction map reveals a scaffold-like complex required for inner membrane organization in mitochondria |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3198156/ https://www.ncbi.nlm.nih.gov/pubmed/21987634 http://dx.doi.org/10.1083/jcb.201107053 |
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