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Mitochondrial ATP synthase: architecture, function and pathology

Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F(1), situated in the mitochondrial matrix, and F(o), located in the inner mitochondrial membrane. Complex V uses the energy created by the proton electrochemical gradient to phosphorylate ADP to ATP. This review...

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Detalles Bibliográficos
Autores principales: Jonckheere, An I., Smeitink, Jan A. M., Rodenburg, Richard J. T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3278611/
https://www.ncbi.nlm.nih.gov/pubmed/21874297
http://dx.doi.org/10.1007/s10545-011-9382-9
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author Jonckheere, An I.
Smeitink, Jan A. M.
Rodenburg, Richard J. T.
author_facet Jonckheere, An I.
Smeitink, Jan A. M.
Rodenburg, Richard J. T.
author_sort Jonckheere, An I.
collection PubMed
description Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F(1), situated in the mitochondrial matrix, and F(o), located in the inner mitochondrial membrane. Complex V uses the energy created by the proton electrochemical gradient to phosphorylate ADP to ATP. This review covers the architecture, function and assembly of complex V. The role of complex V di-and oligomerization and its relation with mitochondrial morphology is discussed. Finally, pathology related to complex V deficiency and current therapeutic strategies are highlighted. Despite the huge progress in this research field over the past decades, questions remain to be answered regarding the structure of subunits, the function of the rotary nanomotor at a molecular level, and the human complex V assembly process. The elucidation of more nuclear genetic defects will guide physio(patho)logical studies, paving the way for future therapeutic interventions.
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spelling pubmed-32786112012-02-21 Mitochondrial ATP synthase: architecture, function and pathology Jonckheere, An I. Smeitink, Jan A. M. Rodenburg, Richard J. T. J Inherit Metab Dis Review Human mitochondrial (mt) ATP synthase, or complex V consists of two functional domains: F(1), situated in the mitochondrial matrix, and F(o), located in the inner mitochondrial membrane. Complex V uses the energy created by the proton electrochemical gradient to phosphorylate ADP to ATP. This review covers the architecture, function and assembly of complex V. The role of complex V di-and oligomerization and its relation with mitochondrial morphology is discussed. Finally, pathology related to complex V deficiency and current therapeutic strategies are highlighted. Despite the huge progress in this research field over the past decades, questions remain to be answered regarding the structure of subunits, the function of the rotary nanomotor at a molecular level, and the human complex V assembly process. The elucidation of more nuclear genetic defects will guide physio(patho)logical studies, paving the way for future therapeutic interventions. Springer Netherlands 2011-08-27 2012 /pmc/articles/PMC3278611/ /pubmed/21874297 http://dx.doi.org/10.1007/s10545-011-9382-9 Text en © The Author(s) 2011 https://creativecommons.org/licenses/by-nc/4.0/ This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited.
spellingShingle Review
Jonckheere, An I.
Smeitink, Jan A. M.
Rodenburg, Richard J. T.
Mitochondrial ATP synthase: architecture, function and pathology
title Mitochondrial ATP synthase: architecture, function and pathology
title_full Mitochondrial ATP synthase: architecture, function and pathology
title_fullStr Mitochondrial ATP synthase: architecture, function and pathology
title_full_unstemmed Mitochondrial ATP synthase: architecture, function and pathology
title_short Mitochondrial ATP synthase: architecture, function and pathology
title_sort mitochondrial atp synthase: architecture, function and pathology
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3278611/
https://www.ncbi.nlm.nih.gov/pubmed/21874297
http://dx.doi.org/10.1007/s10545-011-9382-9
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