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Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure

Mitochondria contain connexins, a family of proteins that is known to form gap junction channels. Connexins are synthesized in the endoplasmic reticulum and oligomerized in the Golgi to form hemichannels. Hemichannels from adjacent cells dock with one another to form gap junction channels that aggre...

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Autores principales: Cetin-Ferra, Selma, Francis, Sharon C., Cooper, Anthonya T., Neikirk, Kit, Marshall, Andrea G., Hinton, Antentor, Murray, Sandra A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10219162/
https://www.ncbi.nlm.nih.gov/pubmed/37240383
http://dx.doi.org/10.3390/ijms24109036
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author Cetin-Ferra, Selma
Francis, Sharon C.
Cooper, Anthonya T.
Neikirk, Kit
Marshall, Andrea G.
Hinton, Antentor
Murray, Sandra A.
author_facet Cetin-Ferra, Selma
Francis, Sharon C.
Cooper, Anthonya T.
Neikirk, Kit
Marshall, Andrea G.
Hinton, Antentor
Murray, Sandra A.
author_sort Cetin-Ferra, Selma
collection PubMed
description Mitochondria contain connexins, a family of proteins that is known to form gap junction channels. Connexins are synthesized in the endoplasmic reticulum and oligomerized in the Golgi to form hemichannels. Hemichannels from adjacent cells dock with one another to form gap junction channels that aggregate into plaques and allow cell–cell communication. Cell–cell communication was once thought to be the only function of connexins and their gap junction channels. In the mitochondria, however, connexins have been identified as monomers and assembled into hemichannels, thus questioning their role solely as cell–cell communication channels. Accordingly, mitochondrial connexins have been suggested to play critical roles in the regulation of mitochondrial functions, including potassium fluxes and respiration. However, while much is known about plasma membrane gap junction channel connexins, the presence and function of mitochondrial connexins remain poorly understood. In this review, the presence and role of mitochondrial connexins and mitochondrial/connexin-containing structure contact sites will be discussed. An understanding of the significance of mitochondrial connexins and their connexin contact sites is essential to our knowledge of connexins’ functions in normal and pathological conditions, and this information may aid in the development of therapeutic interventions in diseases linked to mitochondria.
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spelling pubmed-102191622023-05-27 Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure Cetin-Ferra, Selma Francis, Sharon C. Cooper, Anthonya T. Neikirk, Kit Marshall, Andrea G. Hinton, Antentor Murray, Sandra A. Int J Mol Sci Review Mitochondria contain connexins, a family of proteins that is known to form gap junction channels. Connexins are synthesized in the endoplasmic reticulum and oligomerized in the Golgi to form hemichannels. Hemichannels from adjacent cells dock with one another to form gap junction channels that aggregate into plaques and allow cell–cell communication. Cell–cell communication was once thought to be the only function of connexins and their gap junction channels. In the mitochondria, however, connexins have been identified as monomers and assembled into hemichannels, thus questioning their role solely as cell–cell communication channels. Accordingly, mitochondrial connexins have been suggested to play critical roles in the regulation of mitochondrial functions, including potassium fluxes and respiration. However, while much is known about plasma membrane gap junction channel connexins, the presence and function of mitochondrial connexins remain poorly understood. In this review, the presence and role of mitochondrial connexins and mitochondrial/connexin-containing structure contact sites will be discussed. An understanding of the significance of mitochondrial connexins and their connexin contact sites is essential to our knowledge of connexins’ functions in normal and pathological conditions, and this information may aid in the development of therapeutic interventions in diseases linked to mitochondria. MDPI 2023-05-20 /pmc/articles/PMC10219162/ /pubmed/37240383 http://dx.doi.org/10.3390/ijms24109036 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Cetin-Ferra, Selma
Francis, Sharon C.
Cooper, Anthonya T.
Neikirk, Kit
Marshall, Andrea G.
Hinton, Antentor
Murray, Sandra A.
Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure
title Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure
title_full Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure
title_fullStr Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure
title_full_unstemmed Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure
title_short Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure
title_sort mitochondrial connexins and mitochondrial contact sites with gap junction structure
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10219162/
https://www.ncbi.nlm.nih.gov/pubmed/37240383
http://dx.doi.org/10.3390/ijms24109036
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