Drp1 Tubulates the ER in a GTPase-Independent Manner

Yoshihiro Adachi, Takashi Kato, Tatsuya Yamada, Daisuke Murata, Kenta Arai, Robert V. Stahelin, David C. Chan, Miho Iijima, Hiromi Sesaki

Research output: Contribution to journalArticlepeer-review

3 Scopus citations


Mitochondria are highly dynamic organelles that continuously grow, divide, and fuse. The division of mitochondria is crucial for human health. During mitochondrial division, the mechano-guanosine triphosphatase (GTPase) dynamin-related protein (Drp1) severs mitochondria at endoplasmic reticulum (ER)-mitochondria contact sites, where peripheral ER tubules interact with mitochondria. Here, we report that Drp1 directly shapes peripheral ER tubules in human and mouse cells. This ER-shaping activity is independent of GTP hydrolysis and located in a highly conserved peptide of 18 amino acids (termed D-octadecapeptide), which is predicted to form an amphipathic α helix. Synthetic D-octadecapeptide tubulates liposomes in vitro and the ER in cells. ER tubules formed by Drp1 promote mitochondrial division by facilitating ER-mitochondria interactions. Thus, Drp1 functions as a two-in-one protein during mitochondrial division, with ER tubulation and mechano-GTPase activities.

Original languageEnglish (US)
Pages (from-to)621-632.e6
JournalMolecular cell
Issue number4
StatePublished - Nov 19 2020


  • Drp1
  • mitochondria
  • mitochondrial division
  • organelle contact sites
  • phosphaditic acid
  • the endoplasmic reticulum

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology


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