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The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology
The inner membrane (IM) of mitochondria displays an intricate, highly folded architecture and can be divided into two domains: the inner boundary membrane adjacent to the outer membrane and invaginations toward the matrix, called cristae. Both domains are connected by narrow, tubular membrane segmen...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5379949/ https://www.ncbi.nlm.nih.gov/pubmed/28254827 http://dx.doi.org/10.1083/jcb.201609046 |
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author | Tarasenko, Daryna Barbot, Mariam Jans, Daniel C. Kroppen, Benjamin Sadowski, Boguslawa Heim, Gudrun Möbius, Wiebke Jakobs, Stefan Meinecke, Michael |
author_facet | Tarasenko, Daryna Barbot, Mariam Jans, Daniel C. Kroppen, Benjamin Sadowski, Boguslawa Heim, Gudrun Möbius, Wiebke Jakobs, Stefan Meinecke, Michael |
author_sort | Tarasenko, Daryna |
collection | PubMed |
description | The inner membrane (IM) of mitochondria displays an intricate, highly folded architecture and can be divided into two domains: the inner boundary membrane adjacent to the outer membrane and invaginations toward the matrix, called cristae. Both domains are connected by narrow, tubular membrane segments called cristae junctions (CJs). The formation and maintenance of CJs is of vital importance for the organization of the mitochondrial IM and for mitochondrial and cellular physiology. The multisubunit mitochondrial contact site and cristae organizing system (MICOS) was found to be a major factor in CJ formation. In this study, we show that the MICOS core component Mic60 actively bends membranes and, when inserted into prokaryotic membranes, induces the formation of cristae-like plasma membrane invaginations. The intermembrane space domain of Mic60 has a lipid-binding capacity and induces membrane curvature even in the absence of the transmembrane helix. Mic60 homologues from α-proteobacteria display the same membrane deforming activity and are able to partially overcome the deletion of Mic60 in eukaryotic cells. Our results show that membrane bending by Mic60 is an ancient mechanism, important for cristae formation, and had already evolved before α-proteobacteria developed into mitochondria. |
format | Online Article Text |
id | pubmed-5379949 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-53799492017-10-03 The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology Tarasenko, Daryna Barbot, Mariam Jans, Daniel C. Kroppen, Benjamin Sadowski, Boguslawa Heim, Gudrun Möbius, Wiebke Jakobs, Stefan Meinecke, Michael J Cell Biol Research Articles The inner membrane (IM) of mitochondria displays an intricate, highly folded architecture and can be divided into two domains: the inner boundary membrane adjacent to the outer membrane and invaginations toward the matrix, called cristae. Both domains are connected by narrow, tubular membrane segments called cristae junctions (CJs). The formation and maintenance of CJs is of vital importance for the organization of the mitochondrial IM and for mitochondrial and cellular physiology. The multisubunit mitochondrial contact site and cristae organizing system (MICOS) was found to be a major factor in CJ formation. In this study, we show that the MICOS core component Mic60 actively bends membranes and, when inserted into prokaryotic membranes, induces the formation of cristae-like plasma membrane invaginations. The intermembrane space domain of Mic60 has a lipid-binding capacity and induces membrane curvature even in the absence of the transmembrane helix. Mic60 homologues from α-proteobacteria display the same membrane deforming activity and are able to partially overcome the deletion of Mic60 in eukaryotic cells. Our results show that membrane bending by Mic60 is an ancient mechanism, important for cristae formation, and had already evolved before α-proteobacteria developed into mitochondria. The Rockefeller University Press 2017-04-03 /pmc/articles/PMC5379949/ /pubmed/28254827 http://dx.doi.org/10.1083/jcb.201609046 Text en © 2017 Tarasenko et al. http://www.rupress.org/terms/https://creativecommons.org/licenses/by-nc-sa/4.0/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 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Research Articles Tarasenko, Daryna Barbot, Mariam Jans, Daniel C. Kroppen, Benjamin Sadowski, Boguslawa Heim, Gudrun Möbius, Wiebke Jakobs, Stefan Meinecke, Michael The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
title | The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
title_full | The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
title_fullStr | The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
title_full_unstemmed | The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
title_short | The MICOS component Mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
title_sort | micos component mic60 displays a conserved membrane-bending activity that is necessary for normal cristae morphology |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5379949/ https://www.ncbi.nlm.nih.gov/pubmed/28254827 http://dx.doi.org/10.1083/jcb.201609046 |
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