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J Cell Sci. 2018 Apr 19;132(4). pii: jcs208603. doi: 10.1242/jcs.208603.

Drp1 polymerization stabilizes curved tubular membranes similar to those of constricted mitochondria.

Author information

1
Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany.
2
Biofisika Institute (CSIC, UPV/EHU), Department of Biochemistry and Molecular Biology, University of the Basque Country, 48940 Leioa, Spain.
3
Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, France.
4
Sorbonne Universités, UPMC Univ Paris 06, 75005 Paris, France.
5
Max Planck Institute for Intelligent Systems, 70569 Stuttgart, Germany.

Abstract

Dynamin-related protein 1 (Drp1), an 80 kDa mechanochemical GTPase of the dynamin superfamily, is required for mitochondrial division in mammals. Despite the role of Drp1 dysfunction in human disease, its molecular mechanism remains poorly understood. Here, we examined the effect of Drp1 on membrane curvature using tubes pulled from giant unilamellar vesicles (GUVs). We found that GTP promoted rapid rearrangement of Drp1 from a uniform distribution to discrete foci, in line with the assembly of Drp1 scaffolds at multiple nucleation sites around the lipid tube. Polymerized Drp1 preserved the membrane tube below the protein coat, also in the absence of pulling forces, but did not induce spontaneous membrane fission. Strikingly, Drp1 polymers stabilized membrane curvatures similar to those of constricted mitochondria against pressure changes. Our findings support a new model for mitochondrial division whereby Drp1 mainly acts as a scaffold for membrane curvature stabilization, which sets it apart from other dynamin homologs.

KEYWORDS:

Curvature stabilizer; Dynamin-related protein 1; Membrane biophysics; Membrane curvature; Mitochondrial fission; Protein self-assembly

PMID:
29361534
DOI:
10.1242/jcs.208603
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Conflict of interest statement

Competing interestsThe authors declare no competing or financial interests.

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