Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes

Yuuta Imoto, Yuichi Abe, Masanori Honsho, Kanji Okumoto, Mio Ohnuma, Haruko Kuroiwa, Tsuneyoshi Kuroiwa, Yukio Fujiki

研究成果: Contribution to journalArticle査読

11 被引用数 (Scopus)

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.

本文言語英語
論文番号4634
ジャーナルNature communications
9
1
DOI
出版ステータス出版済み - 12 1 2018

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Physics and Astronomy(all)

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