Evidence map›Paper›PMID 29357276›Full record

ArticleeLife2018

Dynamic clustering of dynamin-amphiphysin helices regulates membrane constriction and fission coupled with GTP hydrolysis.

Tetsuya Takeda, Toshiya Kozai, Huiran Yang, Daiki Ishikuro, Kaho Seyama, Yusuke Kumagai, Tadashi Abe, Hiroshi Yamada, Takayuki Uchihashi, Toshio Ando and 1 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. 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
  4. Article
  5. Review
  6. Article
  7. Review
  8. BIN1 modulation in vivo rescues dynamin-related myopathy.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Recruitment of Irgb6 to the membrane is a direct trigger for membrane deformation.Frontiers in cellular and infection microbiology · 2022
    Article
  10. Article
  11. Neuronal ROS-induced glial lipid droplet formation is altered by loss of Alzheimer's disease-associated genes.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Quantification and demonstration of the collective constriction-by-ratchet mechanism in the dynamin molecular motor.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Review
  16. Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020
    Review
  17. Article
  18. Biophysics in Kanazawa University.Biophysical reviews · 2020
    Article
  19. Article
  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

11 authors at 3 institutions in 1 country.

Tetsuya TakedaGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.ORCID http://orcid.org/0000-0002-3183-6551
Toshiya KozaiDepartment of Physics, College of Science and Engineering, Kanazawa University, Kanazawa, Japan.
Huiran YangGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Daiki IshikuroDepartment of Physics, College of Science and Engineering, Kanazawa University, Kanazawa, Japan.
Kaho SeyamaGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Yusuke KumagaiDepartment of Physics, College of Science and Engineering, Kanazawa University, Kanazawa, Japan.
Tadashi AbeGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Hiroshi YamadaGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Takayuki UchihashiCREST, JST, Saitama, Japan.
Toshio AndoCREST, JST, Saitama, Japan.
Kohji TakeiGraduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama, Japan.
Okayama University · JPKanazawa University · JPJapan Science and Technology Agency · JP

Funding

Japan Science and Technology Agency JPMJCR13M1Japan Society for the Promotion of Science JP15H03540Ministry of Education, Culture, Sports, Science, and Technology JP16H00758Ministry of Education, Culture, Sports, Science, and Technology JP16H00830
6 · The paper itself

Abstract

Dynamin is a mechanochemical GTPase essential for membrane fission during clathrin-mediated endocytosis. Dynamin forms helical complexes at the neck of clathrin-coated pits and their structural changes coupled with GTP hydrolysis drive membrane fission. Dynamin and its binding protein amphiphysin cooperatively regulate membrane remodeling during the fission, but its precise mechanism remains elusive. In this study, we analyzed structural changes of dynamin-amphiphysin complexes during the membrane fission using electron microscopy (EM) and high-speed atomic force microscopy (HS-AFM). Interestingly, HS-AFM analyses show that the dynamin-amphiphysin helices are rearranged to form clusters upon GTP hydrolysis and membrane constriction occurs at protein-uncoated regions flanking the clusters. We also show a novel function of amphiphysin in size control of the clusters to enhance biogenesis of endocytic vesicles. Our approaches using combination of EM and HS-AFM clearly demonstrate new mechanistic insights into the dynamics of dynamin-amphiphysin complexes during membrane fission.

Indexed as

EndocytosisAnimalsDynamin IGuanosine TriphosphateHumansHydrolysisMembranesMicroscopy, Atomic ForceMicroscopy, ElectronNerve Tissue ProteinsSf9 CellsSpodopteraamphiphysinDynamin IGuanosine TriphosphateNerve Tissue Proteinsamphiphysinbiophysicscell biologydynaminEMHS-AFMhumanin vitro reconstitutionmembrane remodelingstructural biology

Identifiers

PMID29357276
PMCPMC5780043
OpenAlexW2953104539

What OpenQuestion holds

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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.