Evidence map›Paper›PMID 25237193›Full record

ArticleThe Journal of biological chemistry2014

Dynamin-related protein 1 (Drp1) promotes structural intermediates of membrane division.

Begoña Ugarte-Uribe, Hans-Michael Müller, Miki Otsuki, Walter Nickel, Ana J García-Sáez

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

48 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. The Structure of the Drp1 Lattice on Membrane.Journal of molecular biology · 2025
    Article
  4. Molecular mechanisms of mitochondrial dynamics.Nature reviews. Molecular cell biology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Is Drp1 sufficient to catalyze membrane fission?Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Review
  15. Article
  16. Mitochondrial membranes modify mutant huntingtin aggregation.Biochimica et biophysica acta. Biomembranes · 2021
    Article
  17. Article
  18. NMR identification of a conserved Drp1 cardiolipin-binding motif essential for stress-induced mitochondrial fission.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Begoña Ugarte-UribeMax-Planck Institute for Intelligent Systems, 70569 Stuttgart, Germany,; Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and.
Hans-Michael MüllerHeidelberg University Biochemistry Center, 69120 Heidelberg, Germany.
Miki OtsukiMax-Planck Institute for Intelligent Systems, 70569 Stuttgart, Germany.
Walter NickelHeidelberg University Biochemistry Center, 69120 Heidelberg, Germany.
Ana J García-SáezMax-Planck Institute for Intelligent Systems, 70569 Stuttgart, Germany,; Interfaculty Institute of Biochemistry, University of Tübingen, 72076 Tübingen, Germany, and. Electronic address: ana.garcia@uni-tuebingen.de.
Heidelberg University · DEUniversity of Tübingen · DEMax Planck Institute for Intelligent Systems · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drp1 is a dynamin-like GTPase that mediates mitochondrial and peroxisomal division in a process dependent on self-assembly and coupled to GTP hydrolysis. Despite the link between Drp1 malfunction and human disease, the molecular details of its membrane activity remain poorly understood. Here we reconstituted and directly visualized Drp1 activity in giant unilamellar vesicles. We quantified the effect of lipid composition and GTP on membrane binding and remodeling activity by fluorescence confocal microscopy and flow cytometry. In contrast to other dynamin relatives, Drp1 bound to both curved and flat membranes even in the absence of nucleotides. We also found that Drp1 induced membrane tubulation that was stimulated by cardiolipin. Moreover, Drp1 promoted membrane tethering dependent on the intrinsic curvature of the membrane lipids and on GTP. Interestingly, Drp1 concentrated at membrane contact surfaces and, in the presence of GTP, formed discrete clusters on the vesicles. Our findings support a role of Drp1 not only in the formation of lipid tubes but also on the stabilization of tightly apposed membranes, which are intermediate states in the process of mitochondrial fission.

Indexed as

Mitochondrial DynamicsAnimalsCardiolipinsCells, CulturedDynaminsGuanosine TriphosphateHumansLiposomesMembrane LipidsMiceMitochondrial MembranesProtein BindingProtein Structure, QuaternaryProtein TransportCardiolipinsDnm1l protein, mouseDynaminsGuanosine TriphosphateLiposomesMembrane LipidsGiant Unilamellar VesiclesGTPaseLiposomeMembrane BiophysicsMembrane CurvatureMembrane FissionMembrane ReconstitutionMitochondria

Identifiers

PMID25237193
PMCPMC4215243
OpenAlexW2042609726

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.