The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation

Oxidative phosphorylation takes place at specialized compartments of the inner mitochondrial membrane, the cristae. The elaborate ultrastructure of cristae membranes enables efficient chemi-osmotic coupling of respiratory chain and F(1)F(o)-ATP synthase. Dynamic membrane remodeling allows mitochondr...

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Autores principales: Rampelt, Heike, van der Laan, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Shared Science Publishers OG 2017
Materias:
Microbiology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568429/
https://www.ncbi.nlm.nih.gov/pubmed/28845421
http://dx.doi.org/10.15698/mic2017.08.583
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author Rampelt, Heike
van der Laan, Martin
author_facet Rampelt, Heike
van der Laan, Martin
author_sort Rampelt, Heike
collection PubMed
description Oxidative phosphorylation takes place at specialized compartments of the inner mitochondrial membrane, the cristae. The elaborate ultrastructure of cristae membranes enables efficient chemi-osmotic coupling of respiratory chain and F(1)F(o)-ATP synthase. Dynamic membrane remodeling allows mitochondria to adapt to changing physiological requirements. The mitochondrial contact site and cristae organizing system (MICOS) and the oligomeric ATP synthase have been known to govern distinct features of cristae architecture. A new study 1 on the crosstalk between these two machineries now sheds light on the mechanisms of cristae formation and maintenance.
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spelling pubmed-55684292017-08-26 The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation Rampelt, Heike van der Laan, Martin Microb Cell Microbiology Oxidative phosphorylation takes place at specialized compartments of the inner mitochondrial membrane, the cristae. The elaborate ultrastructure of cristae membranes enables efficient chemi-osmotic coupling of respiratory chain and F(1)F(o)-ATP synthase. Dynamic membrane remodeling allows mitochondria to adapt to changing physiological requirements. The mitochondrial contact site and cristae organizing system (MICOS) and the oligomeric ATP synthase have been known to govern distinct features of cristae architecture. A new study 1 on the crosstalk between these two machineries now sheds light on the mechanisms of cristae formation and maintenance. Shared Science Publishers OG 2017-08-07 /pmc/articles/PMC5568429/ /pubmed/28845421 http://dx.doi.org/10.15698/mic2017.08.583 Text en https://creativecommons.org/licenses/by/4.0/ This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
spellingShingle Microbiology
Rampelt, Heike
van der Laan, Martin
The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation
title The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation
title_full The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation
title_fullStr The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation
title_full_unstemmed The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation
title_short The Yin & Yang of Mitochondrial Architecture - Interplay of MICOS and F(1)F(o)-ATP synthase in cristae formation
title_sort yin & yang of mitochondrial architecture - interplay of micos and f(1)f(o)-atp synthase in cristae formation
topic Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568429/
https://www.ncbi.nlm.nih.gov/pubmed/28845421
http://dx.doi.org/10.15698/mic2017.08.583
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