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Breaking the clip for cargo unloading from motor proteins: mechanism and significance

The mitochondrion is an essential organelle involved in ATP generation, lipid metabolism, regulation of calcium ions, etc. Therefore, it should be inherited properly by newly generated cells. In the budding yeast Saccharomyces cerevisiae, mitochondria are passed on to daughter cells by the motor pro...

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Autores principales: Obara, Keisuke, Kamura, Takumi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Shared Science Publishers OG 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9173699/
https://www.ncbi.nlm.nih.gov/pubmed/35795253
http://dx.doi.org/10.15698/mic2022.06.779
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author Obara, Keisuke
Kamura, Takumi
author_facet Obara, Keisuke
Kamura, Takumi
author_sort Obara, Keisuke
collection PubMed
description The mitochondrion is an essential organelle involved in ATP generation, lipid metabolism, regulation of calcium ions, etc. Therefore, it should be inherited properly by newly generated cells. In the budding yeast Saccharomyces cerevisiae, mitochondria are passed on to daughter cells by the motor protein, Myo2, on the actin cable. The mitochondria and Myo2 are connected via the adaptor protein Mmr1. After reaching daughter cells, mitochondria are released from the actin-myosin machinery and move dynamically. In our recent paper (Obara K et al. (2022), Nat Commun, doi:10.1038/s41467-022-29704-8), we demonstrated that the regulated proteolysis of Mmr1 is required for the unloading of mitochondria from Myo2 in daughter cells. Sequential post-translational modifications of Mmr1, i.e., phosphorylation followed by ubiquitination, are essential for Mmr1 degradation and mitochondrial release from Myo2. Defects in Mmr1 degradation cause stacking and deformation of mitochondria at the bud-tip and bud-neck, where Myo2 accumulates. Compared to wild-type cells, mutant cells with defects in Mmr1 degradation possess an elevated mitochondrial membrane potential and produce higher levels of reactive oxygen species (ROS), along with hypersensitivity to oxidative stress.
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spelling pubmed-91736992022-07-05 Breaking the clip for cargo unloading from motor proteins: mechanism and significance Obara, Keisuke Kamura, Takumi Microb Cell Microreview The mitochondrion is an essential organelle involved in ATP generation, lipid metabolism, regulation of calcium ions, etc. Therefore, it should be inherited properly by newly generated cells. In the budding yeast Saccharomyces cerevisiae, mitochondria are passed on to daughter cells by the motor protein, Myo2, on the actin cable. The mitochondria and Myo2 are connected via the adaptor protein Mmr1. After reaching daughter cells, mitochondria are released from the actin-myosin machinery and move dynamically. In our recent paper (Obara K et al. (2022), Nat Commun, doi:10.1038/s41467-022-29704-8), we demonstrated that the regulated proteolysis of Mmr1 is required for the unloading of mitochondria from Myo2 in daughter cells. Sequential post-translational modifications of Mmr1, i.e., phosphorylation followed by ubiquitination, are essential for Mmr1 degradation and mitochondrial release from Myo2. Defects in Mmr1 degradation cause stacking and deformation of mitochondria at the bud-tip and bud-neck, where Myo2 accumulates. Compared to wild-type cells, mutant cells with defects in Mmr1 degradation possess an elevated mitochondrial membrane potential and produce higher levels of reactive oxygen species (ROS), along with hypersensitivity to oxidative stress. Shared Science Publishers OG 2022-05-19 /pmc/articles/PMC9173699/ /pubmed/35795253 http://dx.doi.org/10.15698/mic2022.06.779 Text en Copyright: © 2022 Obara and Kamura. https://creativecommons.org/licenses/by/4.0/This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
spellingShingle Microreview
Obara, Keisuke
Kamura, Takumi
Breaking the clip for cargo unloading from motor proteins: mechanism and significance
title Breaking the clip for cargo unloading from motor proteins: mechanism and significance
title_full Breaking the clip for cargo unloading from motor proteins: mechanism and significance
title_fullStr Breaking the clip for cargo unloading from motor proteins: mechanism and significance
title_full_unstemmed Breaking the clip for cargo unloading from motor proteins: mechanism and significance
title_short Breaking the clip for cargo unloading from motor proteins: mechanism and significance
title_sort breaking the clip for cargo unloading from motor proteins: mechanism and significance
topic Microreview
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9173699/
https://www.ncbi.nlm.nih.gov/pubmed/35795253
http://dx.doi.org/10.15698/mic2022.06.779
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