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Research Article
Drp1 polymerization stabilizes curved tubular membranes similar to those of constricted mitochondria
Begoña Ugarte-Uribe, Coline Prévost, Kushal Kumar Das, Patricia Bassereau, Ana J. García-Sáez
J Cell Sci 2017 : jcs.208603 doi: 10.1242/jcs.208603 Published 19 December 2017
Begoña Ugarte-Uribe
Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, GermanyBiofisika Institute (CSIC, UPV/EHU), Department of Biochemistry and Molecular Biology, University of the Basque Country, 48940 Leioa, Spain
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Coline Prévost
Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, FranceSorbonne Universités, UPMC Univ Paris 06, 75005 Paris, France
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Kushal Kumar Das
Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany
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Patricia Bassereau
Laboratoire Physico Chimie Curie, Institut Curie, PSL Research University, CNRS UMR168, 75005 Paris, FranceSorbonne Universités, UPMC Univ Paris 06, 75005 Paris, France
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Ana J. García-Sáez
Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, GermanyMax Planck Institute for Intelligent Systems, 70569 Stuttgart, Germany
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  • For correspondence: ana.garcia@uni-tuebingen.de
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Abstract

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 as a minimal machinery on membrane curvature using tubes pulled from 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 where Drp1 mainly acts as a scaffold for membrane curvature stabilization, which sets it apart from other dynamin homologs.

  • Received July 14, 2017.
  • Accepted December 5, 2017.
  • © 2017. Published by The Company of Biologists Ltd
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Keywords

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

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Drp1 polymerization stabilizes curved tubular membranes similar to those of constricted mitochondria
Begoña Ugarte-Uribe, Coline Prévost, Kushal Kumar Das, Patricia Bassereau, Ana J. García-Sáez
J Cell Sci 2017 : jcs.208603 doi: 10.1242/jcs.208603 Published 19 December 2017
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Drp1 polymerization stabilizes curved tubular membranes similar to those of constricted mitochondria
Begoña Ugarte-Uribe, Coline Prévost, Kushal Kumar Das, Patricia Bassereau, Ana J. García-Sáez
J Cell Sci 2017 : jcs.208603 doi: 10.1242/jcs.208603 Published 19 December 2017

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