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Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria
Microtubules are essential components of the cytoskeleton that allow bi-lateral neuronal transport. Correct regulation of these complex intracellular transport processes is central to neuronal function. However, despite major advancements in our knowledge, we still lack a complete understanding on h...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9638805/ https://www.ncbi.nlm.nih.gov/pubmed/36353120 http://dx.doi.org/10.17912/micropub.biology.000659 |
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author | Teoh, Jean-Sébastien Dhananjay, Samiksha Neumann, Brent |
author_facet | Teoh, Jean-Sébastien Dhananjay, Samiksha Neumann, Brent |
author_sort | Teoh, Jean-Sébastien |
collection | PubMed |
description | Microtubules are essential components of the cytoskeleton that allow bi-lateral neuronal transport. Correct regulation of these complex intracellular transport processes is central to neuronal function. However, despite major advancements in our knowledge, we still lack a complete understanding on how neuronal transport is regulated. Here, we provide further evidence for the importance of the highly conserved N-terminal H12-helix of α-tubulin. We show that a mutation in this region results in the mistargeting of axonal mitochondria in Caenorhabditis elegans , thereby establishing the importance of the H12-helix in regulating mitochondrial transport in neurons. |
format | Online Article Text |
id | pubmed-9638805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-96388052022-11-08 Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria Teoh, Jean-Sébastien Dhananjay, Samiksha Neumann, Brent MicroPubl Biol New Finding Microtubules are essential components of the cytoskeleton that allow bi-lateral neuronal transport. Correct regulation of these complex intracellular transport processes is central to neuronal function. However, despite major advancements in our knowledge, we still lack a complete understanding on how neuronal transport is regulated. Here, we provide further evidence for the importance of the highly conserved N-terminal H12-helix of α-tubulin. We show that a mutation in this region results in the mistargeting of axonal mitochondria in Caenorhabditis elegans , thereby establishing the importance of the H12-helix in regulating mitochondrial transport in neurons. Caltech Library 2022-10-23 /pmc/articles/PMC9638805/ /pubmed/36353120 http://dx.doi.org/10.17912/micropub.biology.000659 Text en Copyright: © 2022 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Teoh, Jean-Sébastien Dhananjay, Samiksha Neumann, Brent Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria |
title | Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria |
title_full | Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria |
title_fullStr | Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria |
title_full_unstemmed | Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria |
title_short | Mutation of the H12-helix of α-tubulin/MEC-12 disrupts the localization of neuronal mitochondria |
title_sort | mutation of the h12-helix of α-tubulin/mec-12 disrupts the localization of neuronal mitochondria |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9638805/ https://www.ncbi.nlm.nih.gov/pubmed/36353120 http://dx.doi.org/10.17912/micropub.biology.000659 |
work_keys_str_mv | AT teohjeansebastien mutationoftheh12helixofatubulinmec12disruptsthelocalizationofneuronalmitochondria AT dhananjaysamiksha mutationoftheh12helixofatubulinmec12disruptsthelocalizationofneuronalmitochondria AT neumannbrent mutationoftheh12helixofatubulinmec12disruptsthelocalizationofneuronalmitochondria |