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

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article number4634
JournalNature communications
Volume9
Issue number1
DOIs
Publication statusPublished - Dec 1 2018

Fingerprint

Dynamins
Mitochondria
Fueling
Peroxisomes
mitochondria
refueling
Guanosine Triphosphate
division
rings
machinery
Machinery
Constriction
Nucleoside-Diphosphate Kinase
constrictions
Mitochondrial Dynamics
Membranes
eukaryotes
membranes
diphosphates
GTP Phosphohydrolases

All Science Journal Classification (ASJC) codes

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

Cite this

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.

In: Nature communications, Vol. 9, No. 1, 4634, 01.12.2018.

Research output: Contribution to journalArticle

Imoto, Y, Abe, Y, Honsho, M, Okumoto, K, Ohnuma, M, Kuroiwa, H, Kuroiwa, T & Fujiki, Y 2018, 'Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes', Nature communications, vol. 9, no. 1, 4634. https://doi.org/10.1038/s41467-018-07009-z
Imoto, Yuuta ; Abe, Yuichi ; Honsho, Masanori ; Okumoto, Kanji ; Ohnuma, Mio ; Kuroiwa, Haruko ; Kuroiwa, Tsuneyoshi ; Fujiki, Yukio. / Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes. In: Nature communications. 2018 ; Vol. 9, No. 1.
@article{c9539949e9e94525b788493da35831fa,
title = "Onsite GTP fuelling via DYNAMO1 drives division of mitochondria and peroxisomes",
abstract = "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.",
author = "Yuuta Imoto and Yuichi Abe and Masanori Honsho and Kanji Okumoto and Mio Ohnuma and Haruko Kuroiwa and Tsuneyoshi Kuroiwa and Yukio Fujiki",
year = "2018",
month = "12",
day = "1",
doi = "10.1038/s41467-018-07009-z",
language = "English",
volume = "9",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=85056093849&partnerID=8YFLogxK

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 -