Molecular Basis of Mitochondrial and Peroxisomal Division Machineries
Mitochondria and peroxisomes are ubiquitous subcellular organelles that are highly dynamic and possess a high degree of plasticity. These organelles proliferate through division of pre-existing organelles. Studies on yeast, mammalian cells, and unicellular algae have led to a surprising finding that...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/21/15/5452 |
| _version_ | 1797560789599518720 |
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| author | Yuuta Imoto Kie Itoh Yukio Fujiki |
| author_facet | Yuuta Imoto Kie Itoh Yukio Fujiki |
| author_sort | Yuuta Imoto |
| collection | DOAJ |
| description | Mitochondria and peroxisomes are ubiquitous subcellular organelles that are highly dynamic and possess a high degree of plasticity. These organelles proliferate through division of pre-existing organelles. Studies on yeast, mammalian cells, and unicellular algae have led to a surprising finding that mitochondria and peroxisomes share the components of their division machineries. At the heart of the mitochondrial and peroxisomal division machineries is a GTPase dynamin-like protein, Dnm1/Drp1, which forms a contractile ring around the neck of the dividing organelles. During division, Dnm1/Drp1 functions as a motor protein and constricts the membrane. This mechanochemical work is achieved by utilizing energy from GTP hydrolysis. Over the last two decades, studies have focused on the structure and assembly of Dnm1/Drp1 molecules around the neck. However, the regulation of GTP during the division of mitochondrion and peroxisome is not well understood. Here, we review the current understanding of Dnm1/Drp1-mediated divisions of mitochondria and peroxisomes, exploring the mechanisms of GTP regulation during the Dnm1/Drp1 function, and provide new perspectives on their potential contribution to mitochondrial and peroxisomal biogenesis. |
| first_indexed | 2024-03-10T18:05:25Z |
| format | Article |
| id | doaj.art-a0a0eccd633947bba516b0ab9efc31b0 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T18:05:25Z |
| publishDate | 2020-07-01 |
| publisher | MDPI AG |
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| series | International Journal of Molecular Sciences |
| spelling | doaj.art-a0a0eccd633947bba516b0ab9efc31b02023-11-20T08:33:39ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-07-012115545210.3390/ijms21155452Molecular Basis of Mitochondrial and Peroxisomal Division MachineriesYuuta Imoto0Kie Itoh1Yukio Fujiki2Department of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USADepartment of Cell Biology, Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USADivision of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, JapanMitochondria and peroxisomes are ubiquitous subcellular organelles that are highly dynamic and possess a high degree of plasticity. These organelles proliferate through division of pre-existing organelles. Studies on yeast, mammalian cells, and unicellular algae have led to a surprising finding that mitochondria and peroxisomes share the components of their division machineries. At the heart of the mitochondrial and peroxisomal division machineries is a GTPase dynamin-like protein, Dnm1/Drp1, which forms a contractile ring around the neck of the dividing organelles. During division, Dnm1/Drp1 functions as a motor protein and constricts the membrane. This mechanochemical work is achieved by utilizing energy from GTP hydrolysis. Over the last two decades, studies have focused on the structure and assembly of Dnm1/Drp1 molecules around the neck. However, the regulation of GTP during the division of mitochondrion and peroxisome is not well understood. Here, we review the current understanding of Dnm1/Drp1-mediated divisions of mitochondria and peroxisomes, exploring the mechanisms of GTP regulation during the Dnm1/Drp1 function, and provide new perspectives on their potential contribution to mitochondrial and peroxisomal biogenesis.https://www.mdpi.com/1422-0067/21/15/5452mitochondrial divisionperoxisomal divisiondynamin-related protein Dnm1/Drp1nucleoside-diphosphate kinaselocal GTP generation |
| spellingShingle | Yuuta Imoto Kie Itoh Yukio Fujiki Molecular Basis of Mitochondrial and Peroxisomal Division Machineries International Journal of Molecular Sciences mitochondrial division peroxisomal division dynamin-related protein Dnm1/Drp1 nucleoside-diphosphate kinase local GTP generation |
| title | Molecular Basis of Mitochondrial and Peroxisomal Division Machineries |
| title_full | Molecular Basis of Mitochondrial and Peroxisomal Division Machineries |
| title_fullStr | Molecular Basis of Mitochondrial and Peroxisomal Division Machineries |
| title_full_unstemmed | Molecular Basis of Mitochondrial and Peroxisomal Division Machineries |
| title_short | Molecular Basis of Mitochondrial and Peroxisomal Division Machineries |
| title_sort | molecular basis of mitochondrial and peroxisomal division machineries |
| topic | mitochondrial division peroxisomal division dynamin-related protein Dnm1/Drp1 nucleoside-diphosphate kinase local GTP generation |
| url | https://www.mdpi.com/1422-0067/21/15/5452 |
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