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Cyclophilin D: An Integrator of Mitochondrial Function

Cyclophilin D (CypD) is a mitochondrial peptidyl-prolyl cis-trans isomerase, well-known for regulating the mitochondrial permeability transition pore (PTP), a nonspecific large conductance pore whose opening leads to cell death and has been implicated in ischemia/reperfusion injury in multiple organ...

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Autores principales: Amanakis, Georgios, Murphy, Elizabeth
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311779/
https://www.ncbi.nlm.nih.gov/pubmed/32625108
http://dx.doi.org/10.3389/fphys.2020.00595
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author Amanakis, Georgios
Murphy, Elizabeth
author_facet Amanakis, Georgios
Murphy, Elizabeth
author_sort Amanakis, Georgios
collection PubMed
description Cyclophilin D (CypD) is a mitochondrial peptidyl-prolyl cis-trans isomerase, well-known for regulating the mitochondrial permeability transition pore (PTP), a nonspecific large conductance pore whose opening leads to cell death and has been implicated in ischemia/reperfusion injury in multiple organs, in neurodegenerative disorders, and in muscular dystrophies. While the main target of CypD is a matter of ongoing research, inhibiting CypD protects in models of those diseases making it an interesting therapeutic target. The present review focuses on post-translational modifications of CypD that have been identified by recent studies, which can alter the regulation of the PTP and contribute to understanding the mechanisms of action of CypD.
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spelling pubmed-73117792020-07-02 Cyclophilin D: An Integrator of Mitochondrial Function Amanakis, Georgios Murphy, Elizabeth Front Physiol Physiology Cyclophilin D (CypD) is a mitochondrial peptidyl-prolyl cis-trans isomerase, well-known for regulating the mitochondrial permeability transition pore (PTP), a nonspecific large conductance pore whose opening leads to cell death and has been implicated in ischemia/reperfusion injury in multiple organs, in neurodegenerative disorders, and in muscular dystrophies. While the main target of CypD is a matter of ongoing research, inhibiting CypD protects in models of those diseases making it an interesting therapeutic target. The present review focuses on post-translational modifications of CypD that have been identified by recent studies, which can alter the regulation of the PTP and contribute to understanding the mechanisms of action of CypD. Frontiers Media S.A. 2020-06-17 /pmc/articles/PMC7311779/ /pubmed/32625108 http://dx.doi.org/10.3389/fphys.2020.00595 Text en Copyright © 2020 Amanakis and Murphy. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Physiology
Amanakis, Georgios
Murphy, Elizabeth
Cyclophilin D: An Integrator of Mitochondrial Function
title Cyclophilin D: An Integrator of Mitochondrial Function
title_full Cyclophilin D: An Integrator of Mitochondrial Function
title_fullStr Cyclophilin D: An Integrator of Mitochondrial Function
title_full_unstemmed Cyclophilin D: An Integrator of Mitochondrial Function
title_short Cyclophilin D: An Integrator of Mitochondrial Function
title_sort cyclophilin d: an integrator of mitochondrial function
topic Physiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7311779/
https://www.ncbi.nlm.nih.gov/pubmed/32625108
http://dx.doi.org/10.3389/fphys.2020.00595
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