Evidence map›Paper›PMID 29022874›Full record

ArticleeLife2017

Uncoupling of dynamin polymerization and GTPase activity revealed by the conformation-specific nanobody dynab.

Valentina Galli, Rafael Sebastian, Sandrine Moutel, Jason Ecard, Franck Perez, Aurélien Roux

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

  1. Nanoscale dynamics of Dynamin 1 helices reveals squeeze-twist deformation mode critical for membrane fission.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Review
  4. Regulation of membrane scission in yeast endocytosis.Molecular biology of the cell · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. Exploring cellular biochemistry with nanobodies.The Journal of biological chemistry · 2020
    Review
  9. Applying Antibodies Inside Cells: Principles and Recent Advances in Neurobiology, Virology and Oncology.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020
    Review
  10. The tilted helix model of dynamin oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. 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

6 authors at 3 institutions in 3 countries.

Valentina GalliDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.
Rafael SebastianDepartment of Computer Sciences, Universidad de Valencia, Valencia, Spain.
Sandrine MoutelInstitut Curie, PSL Research University, Paris, France.
Jason EcardInstitut Curie, PSL Research University, Paris, France.
Franck PerezInstitut Curie, PSL Research University, Paris, France.ORCID http://orcid.org/0000-0002-9129-9401
Aurélien RouxDepartment of Biochemistry, University of Geneva, Geneva, Switzerland.ORCID http://orcid.org/0000-0002-6088-0711
Université Paris Sciences et Lettres · FRUniversity of Geneva · CHUniversitat de València · ES

Funding

European Research Council 311536
6 · The paper itself

Abstract

Dynamin is a large GTPase that forms a helical collar at the neck of endocytic pits, and catalyzes membrane fission (Schmid and Frolov, 2011; Ferguson and De Camilli, 2012). Dynamin fission reaction is strictly dependent on GTP hydrolysis, but how fission is mediated is still debated (Antonny et al., 2016): GTP energy could be spent in membrane constriction required for fission, or in disassembly of the dynamin polymer to trigger fission. To follow dynamin GTP hydrolysis at endocytic pits, we generated a conformation-specific nanobody called dynab, that binds preferentially to the GTP hydrolytic state of dynamin-1. Dynab allowed us to follow the GTPase activity of dynamin-1 in real-time. We show that in fibroblasts, dynamin GTP hydrolysis occurs as stochastic bursts, which are randomly distributed relatively to the peak of dynamin assembly. Thus, dynamin disassembly is not coupled to GTPase activity, supporting that the GTP energy is primarily spent in constriction.

Indexed as

PolymerizationDynamin IFibroblastsGTP PhosphohydrolasesGuanosine TriphosphateHumansHydrolysisSingle-Domain AntibodiesDynamin IGTP PhosphohydrolasesGuanosine TriphosphateSingle-Domain Antibodiescell biologyconformational-specific nanobodydynaminendocytosisenzymehumanmouse

Identifiers

PMID29022874
PMCPMC5658065
OpenAlexW2761193853

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.