| First Author | Adachi Y | Year | 2020 |
| Journal | Mol Cell | Volume | 80 |
| Issue | 4 | Pages | 621-632.e6 |
| PubMed ID | 33152269 | Mgi Jnum | J:300166 |
| Mgi Id | MGI:6489719 | Doi | 10.1016/j.molcel.2020.10.013 |
| Citation | Adachi Y, et al. (2020) Drp1 Tubulates the ER in a GTPase-Independent Manner. Mol Cell 80(4):621-632.e6 |
| abstractText | 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 alpha 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. |
