Evidence map›Paper›PMID 28035046›Full record

ArticleMolecular biology of the cell2017

The pleckstrin-homology domain of dynamin is dispensable for membrane constriction and fission.

Srishti Dar, Thomas J Pucadyil

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Mitochondrial Membrane Remodeling.Frontiers in bioengineering and biotechnology · 2021
    Review
  11. Article
  12. Review
  13. The tilted helix model of dynamin oligomers.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Topography design in model membranes: Where biology meets physics.Experimental biology and medicine (Maywood, N.J.) · 2019
    Review
  15. Article
  16. Article
  17. Article
  18. The 2018 biomembrane curvature and remodeling roadmap.Journal of physics D: Applied physics · 2018
    Article
  19. 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

2 authors at 1 institution in 1 country.

Srishti DarIndian Institute of Science Education and Research, Pashan, Pune Maharashtra 411008, India.
Thomas J PucadyilIndian Institute of Science Education and Research, Pashan, Pune Maharashtra 411008, India pucadyil@iiserpune.ac.in.
Indian Institute of Science Education and Research Pune · IN

Funding

DBT-Wellcome Trust India Alliance 500174-Z-09-ZWellcome Trust
6 · The paper itself

Abstract

Classical dynamins bind the plasma membrane-localized phosphatidylinositol-4,5-bisphosphate using the pleckstrin-homology domain (PHD) and engage in rapid membrane fission during synaptic vesicle recycling. This domain is conspicuously absent among extant bacterial and mitochondrial dynamins, however, where loop regions manage membrane recruitment. Inspired by the core design of bacterial and mitochondrial dynamins, we reengineered the classical dynamin by replacing its PHD with a polyhistidine or polylysine linker. Remarkably, when recruited via chelator or anionic lipids, respectively, the reengineered dynamin displayed the capacity to constrict and sever membrane tubes. However, when analyzed at single-event resolution, the tube-severing process displayed long-lived, highly constricted prefission intermediates that contributed to 10-fold reduction in bulk rates of membrane fission. Our results indicate that the PHD acts as a catalyst in dynamin-induced membrane fission and rationalize its adoption to meet the physiologic requirement of a fast-acting membrane fission apparatus.

Indexed as

Cell MembraneConstrictionDynaminsEndocytosisGTP PhosphohydrolasesGuanosine TriphosphateHumansMembranesMitochondriaMitochondrial DynamicsPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositolsPleckstrin Homology DomainsProtein DomainsProtein Structure, TertiaryDynaminsGTP PhosphohydrolasesGuanosine TriphosphatePhosphatidylinositol 4,5-DiphosphatePhosphatidylinositols

Identifiers

PMID28035046
PMCPMC5221619
OpenAlexW2553122157

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.