Who and how in the regulation of mitochondrial cristae shape and function

Mitochondrial adaptation to different physiological conditions highly relies on the regulation of mitochondrial ultrastructure, particularly at the level of cristae compartment. Cristae represent the membrane hub where most of the respiratory complexes embed to account for OXPHOS and energy producti...

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Detalles Bibliográficos
Autores: Quintana-Cabrera, Ruben, Mehrotra, Anjali, Rigoni, G., Soriano, M.E.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/377823
Acceso en línea:http://hdl.handle.net/10261/377823
Access Level:acceso abierto
Palabra clave:ATP synthase dimers
Cristae ultrastructure
MICOS
Mitochondria
OPA1.
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spelling Who and how in the regulation of mitochondrial cristae shape and functionQuintana-Cabrera, RubenMehrotra, AnjaliRigoni, G.Soriano, M.E.ATP synthase dimersCristae ultrastructureMICOSMitochondriaOPA1.Mitochondrial adaptation to different physiological conditions highly relies on the regulation of mitochondrial ultrastructure, particularly at the level of cristae compartment. Cristae represent the membrane hub where most of the respiratory complexes embed to account for OXPHOS and energy production in the form of adenosine triphosphate (ATP). Changes in cristae number and shape define the respiratory capacity as well as cell viability. The identification of key regulators of cristae morphology and the understanding of their contribution to the mitochondrial ultrastructure and function have become an strategic goal to understand mitochondrial disorders and to exploit as therapeutic targets. This review summarizes the known regulators of cristae ultrastructure and discusses their contribution and implications for mitochondrial dysfunction.We thank Dr.F.Caicci (EM Facility, Dept. of Biology, University of Padova) for EM images. AM is recipient of an IBRO (International Brain Research Organization e International Society for Neurochemistry) research fellowship (2016). R.Q-C was supported by a Fondazione Veronesi Fellowship.Academic PressInternational Brain Research OrganizationInternational Society for NeurochemistryFondazione Umberto VeronesiConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2025202520182025info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_dcae04bcPublisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/377823reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttp://dx.doi.org/10.1016/j.bbrc.2017.04.088Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3778232026-05-22T06:33:51Z
dc.title.none.fl_str_mv Who and how in the regulation of mitochondrial cristae shape and function
title Who and how in the regulation of mitochondrial cristae shape and function
spellingShingle Who and how in the regulation of mitochondrial cristae shape and function
Quintana-Cabrera, Ruben
ATP synthase dimers
Cristae ultrastructure
MICOS
Mitochondria
OPA1.
title_short Who and how in the regulation of mitochondrial cristae shape and function
title_full Who and how in the regulation of mitochondrial cristae shape and function
title_fullStr Who and how in the regulation of mitochondrial cristae shape and function
title_full_unstemmed Who and how in the regulation of mitochondrial cristae shape and function
title_sort Who and how in the regulation of mitochondrial cristae shape and function
dc.creator.none.fl_str_mv Quintana-Cabrera, Ruben
Mehrotra, Anjali
Rigoni, G.
Soriano, M.E.
author Quintana-Cabrera, Ruben
author_facet Quintana-Cabrera, Ruben
Mehrotra, Anjali
Rigoni, G.
Soriano, M.E.
author_role author
author2 Mehrotra, Anjali
Rigoni, G.
Soriano, M.E.
author2_role author
author
author
dc.contributor.none.fl_str_mv International Brain Research Organization
International Society for Neurochemistry
Fondazione Umberto Veronesi
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv ATP synthase dimers
Cristae ultrastructure
MICOS
Mitochondria
OPA1.
topic ATP synthase dimers
Cristae ultrastructure
MICOS
Mitochondria
OPA1.
description Mitochondrial adaptation to different physiological conditions highly relies on the regulation of mitochondrial ultrastructure, particularly at the level of cristae compartment. Cristae represent the membrane hub where most of the respiratory complexes embed to account for OXPHOS and energy production in the form of adenosine triphosphate (ATP). Changes in cristae number and shape define the respiratory capacity as well as cell viability. The identification of key regulators of cristae morphology and the understanding of their contribution to the mitochondrial ultrastructure and function have become an strategic goal to understand mitochondrial disorders and to exploit as therapeutic targets. This review summarizes the known regulators of cristae ultrastructure and discusses their contribution and implications for mitochondrial dysfunction.
publishDate 2018
dc.date.none.fl_str_mv 2018
2025
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_dcae04bc
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/377823
url http://hdl.handle.net/10261/377823
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv http://dx.doi.org/10.1016/j.bbrc.2017.04.088
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Academic Press
publisher.none.fl_str_mv Academic Press
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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