Molecular basis of local energy generation during mitochondrial and peroxisomal division
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- Imoto Yuuta
- Department of Cell Biology, Johns Hopkins University School of Medicine Division of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University
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- Abe Yuichi
- Division of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University
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- Honsho Masanori
- Division of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University
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- Okumoto Kanji
- Department of Biology, Faculty of Sciences, Kyushu University
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- Ohnuma Mio
- National Institute of Technology Hiroshima College
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- Kuroiwa Haruko
- Department of Chemical and Biological Science, Faculty of Science, Japan Women’s University
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- Kuroiwa Tsuneyoshi
- Department of Chemical and Biological Science, Faculty of Science, Japan Women’s University
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- Fujiki Yukio
- Division of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University
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Abstract
<p>GTPase dynamin-related protein (Dnm1)-mediated membrane fission is an important membrane remodeling event supporting the proliferation and housekeeping function of semiautonomous organelles such as the mitochondrion and peroxisome. Dnm1 is at the heart of the membrane fission machinery, which constricts the neck of the dividing organelles. Similar to classical dynamin protein, Dnm1 hydrolyzes GTP, an energy source, thereby generating a constriction force to sever the neck. To complete this process, replenishment of GTP to Dnm1 needs to be done in a regulated and timely manner. However, the molecular mechanisms that provide GTP to Dnm1 are not known. In this review, we present the evidence for emerging consensus on Dnm1 function and our recent work demonstrating that: (1) The ATP-GTP converting, nucleoside diphosphate kinase-like protein DYNAMO1 is present in the mitochondrial and peroxisomal membrane fission machinery. (2) DYNAMO1 facilitates enzyme kinetics of Dnm1 and locally provides GTP to Dnm1 on the membrane fission machinery. (3) The membrane fission machinery spends more GTP on constriction than on recruitment, as seen by the in vivo experiments and in vitro reconstitution of the Dnm1 structure. Summarizing these data, this review would help to understand the mechanism by which Dnm1 promotes membrane fission using GTP as an energy source. We also discuss how future research might solve the remaining open questions regarding the energy issues presently under discussion.</p>
Journal
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- PLANT MORPHOLOGY
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PLANT MORPHOLOGY 32 (1), 59-73, 2020
The Japanese Society of Plant Morphology
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Keywords
Details 詳細情報について
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- CRID
- 1390850475732055808
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- NII Article ID
- 130008006485
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- NII Book ID
- AA11315461
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- ISSN
- 18844154
- 09189726
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- NDL BIB ID
- 031740808
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed