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Drp1 Tubulates the ER in a GTPase-Independent Manner
- Source :
- Mol Cell
- Publication Year :
- 2020
-
Abstract
- 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.
- Subjects :
- Dynamins
endocrine system
Peptide
GTPase
Mitochondrion
Biology
Endoplasmic Reticulum
Mitochondrial Dynamics
Article
GTP Phosphohydrolases
03 medical and health sciences
Mice
0302 clinical medicine
Organelle
Animals
Humans
Molecular Biology
030304 developmental biology
chemistry.chemical_classification
Mice, Knockout
0303 health sciences
Endoplasmic reticulum
Cell Biology
In vitro
Amino acid
Cell biology
Mitochondria
chemistry
Triphosphatase
Guanosine Triphosphate
Oligopeptides
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 10974164
- Volume :
- 80
- Issue :
- 4
- Database :
- OpenAIRE
- Journal :
- Molecular cell
- Accession number :
- edsair.doi.dedup.....1f6784a1b8012557f311d9d3d2ab8956