抄録
Mitochondria and peroxisomes proliferate by division. During division, a part of their membrane is pinched off by constriction of the ring-shaped mitochondrial division (MD) and peroxisome-dividing (POD) machinery. This constriction is mediated by a dynamin-like GTPase Dnm1 that requires a large amount of GTP as an energy source. Here, via proteomics of the isolated division machinery, we show that the 17-kDa nucleoside diphosphate kinase-like protein, dynamin-based ring motive-force organizer 1 (DYNAMO1), locally generates GTP in MD and POD machineries. DYNAMO1 is widely conserved among eukaryotes and colocalizes with Dnm1 on the division machineries. DYNAMO1 converts ATP to GTP, and disruption of its activity impairs mitochondrial and peroxisomal fissions. DYNAMO1 forms a ring-shaped complex with Dnm1 and increases the magnitude of the constricting force. Our results identify DYNAMO1 as an essential component of MD and POD machineries, suggesting that local GTP generation in Dnm1-based machinery regulates motive force for membrane severance.
| 元の言語 | 英語 |
|---|---|
| 記事番号 | 4634 |
| ジャーナル | Nature communications |
| 巻 | 9 |
| 発行部数 | 1 |
| DOI | |
| 出版物ステータス | 出版済み - 12 1 2018 |
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All Science Journal Classification (ASJC) codes
- Chemistry(all)
- Biochemistry, Genetics and Molecular Biology(all)
- Physics and Astronomy(all)
これを引用
Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes. / Imoto, Yuuta; Abe, Yuichi; Honsho, Masanori; Okumoto, Kanji; Ohnuma, Mio; Kuroiwa, Haruko; Kuroiwa, Tsuneyoshi; Fujiki, Yukio.
：: Nature communications, 巻 9, 番号 1, 4634, 01.12.2018.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes
AU - Imoto, Yuuta
AU - Abe, Yuichi
AU - Honsho, Masanori
AU - Okumoto, Kanji
AU - Ohnuma, Mio
AU - Kuroiwa, Haruko
AU - Kuroiwa, Tsuneyoshi
AU - Fujiki, Yukio
PY - 2018/12/1
Y1 - 2018/12/1
N2 - Mitochondria and peroxisomes proliferate by division. During division, a part of their membrane is pinched off by constriction of the ring-shaped mitochondrial division (MD) and peroxisome-dividing (POD) machinery. This constriction is mediated by a dynamin-like GTPase Dnm1 that requires a large amount of GTP as an energy source. Here, via proteomics of the isolated division machinery, we show that the 17-kDa nucleoside diphosphate kinase-like protein, dynamin-based ring motive-force organizer 1 (DYNAMO1), locally generates GTP in MD and POD machineries. DYNAMO1 is widely conserved among eukaryotes and colocalizes with Dnm1 on the division machineries. DYNAMO1 converts ATP to GTP, and disruption of its activity impairs mitochondrial and peroxisomal fissions. DYNAMO1 forms a ring-shaped complex with Dnm1 and increases the magnitude of the constricting force. Our results identify DYNAMO1 as an essential component of MD and POD machineries, suggesting that local GTP generation in Dnm1-based machinery regulates motive force for membrane severance.
AB - Mitochondria and peroxisomes proliferate by division. During division, a part of their membrane is pinched off by constriction of the ring-shaped mitochondrial division (MD) and peroxisome-dividing (POD) machinery. This constriction is mediated by a dynamin-like GTPase Dnm1 that requires a large amount of GTP as an energy source. Here, via proteomics of the isolated division machinery, we show that the 17-kDa nucleoside diphosphate kinase-like protein, dynamin-based ring motive-force organizer 1 (DYNAMO1), locally generates GTP in MD and POD machineries. DYNAMO1 is widely conserved among eukaryotes and colocalizes with Dnm1 on the division machineries. DYNAMO1 converts ATP to GTP, and disruption of its activity impairs mitochondrial and peroxisomal fissions. DYNAMO1 forms a ring-shaped complex with Dnm1 and increases the magnitude of the constricting force. Our results identify DYNAMO1 as an essential component of MD and POD machineries, suggesting that local GTP generation in Dnm1-based machinery regulates motive force for membrane severance.
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UR - http://www.scopus.com/inward/citedby.url?scp=85056093849&partnerID=8YFLogxK
U2 - 10.1038/s41467-018-07009-z
DO - 10.1038/s41467-018-07009-z
M3 - Article
C2 - 30401830
AN - SCOPUS:85056093849
VL - 9
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
IS - 1
M1 - 4634
ER -