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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| Format: | Article |
| Language: | English |
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MDPI AG
2023-05-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/10/9036 |
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| author | Selma Cetin-Ferra Sharon C. Francis Anthonya T. Cooper Kit Neikirk Andrea G. Marshall Antentor Hinton Sandra A. Murray |
| author_facet | Selma Cetin-Ferra Sharon C. Francis Anthonya T. Cooper Kit Neikirk Andrea G. Marshall Antentor Hinton Sandra A. Murray |
| author_sort | Selma Cetin-Ferra |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-11T03:38:53Z |
| format | Article |
| id | doaj.art-b8a98fa43b7045e18038ee240984a31a |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T03:38:53Z |
| publishDate | 2023-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-b8a98fa43b7045e18038ee240984a31a2023-11-18T01:46:18ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-05-012410903610.3390/ijms24109036Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction StructureSelma Cetin-Ferra0Sharon C. Francis1Anthonya T. Cooper2Kit Neikirk3Andrea G. Marshall4Antentor Hinton5Sandra A. Murray6Department of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USADepartment of Physiology, Morehouse School of Medicine, Atlanta, GA 30310, USADepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USADepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232, USADepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232, USADepartment of Molecular Physiology and Biophysics, Vanderbilt University, Nashville, TN 37232, USADepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USAMitochondria 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.https://www.mdpi.com/1422-0067/24/10/9036mitochondriaconnexinannular gap junctionscontact sites |
| spellingShingle | Selma Cetin-Ferra Sharon C. Francis Anthonya T. Cooper Kit Neikirk Andrea G. Marshall Antentor Hinton Sandra A. Murray Mitochondrial Connexins and Mitochondrial Contact Sites with Gap Junction Structure International Journal of Molecular Sciences mitochondria connexin annular gap junctions contact sites |
| 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 | mitochondria connexin annular gap junctions contact sites |
| url | https://www.mdpi.com/1422-0067/24/10/9036 |
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