Evidence map›Paper›PMID 1421574›Full record

ArticleMolecular biology of the cell1992

Interaction of dynamin with microtubules: its structure and GTPase activity investigated by using highly purified dynamin.

K Maeda, T Nakata, Y Noda, R Sato-Yoshitake, N Hirokawa

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Membrane remodeling properties of the Parkinson's disease protein LRRK2.Proceedings of the National Academy of Sciences of the United States of America · 2023
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  12. Dynamics of the sealing zone in cultured osteoclasts.Cytoskeleton (Hoboken, N.J.) · 2017
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  13. Article
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  15. Article
  16. Article
  17. Dynamin rings: not just for fission.Traffic (Copenhagen, Denmark) · 2013
    Review
  18. Review
  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

5 authors at 1 institution in 1 country.

K MaedaDepartment of Anatomy and Cell Biology, School of Medicine, University of Tokyo, Japan.
T Nakata
Y Noda
R Sato-Yoshitake
N Hirokawa
Tokyo University of Agriculture · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We purified a large amount of dynamin with high enzymatical activity from rat brain tissue by a new procedure. Dynamin 0.48 mg was obtained from 20 g of rat brain. The purity of dynamin was almost 98%. Dynamin plays a role of GTPase rather than ATPase. In the absence of microtubules, Michaelis constant (Km) and maximum velocity (Vmax) for dynamin GTPase were 370 microM and 0.25 min-1, respectively, and in their presence, both were significantly accelerated up to 25 microM and 5.5 min-1. On the other hand, the ATPase activity was very low in the absence of microtubules, and even in their presence, Km and Vmax for dynamin ATPase were 0.2 mM and 0.91 min-1. Despite slow GTPase turnover rate in the absence of microtubules, binding of GTP and its nonhydrolizing analogues was very fast, indicating that GTP binding step is not rate limiting. Dynamin did not cause a one-directional consistent microtubule sliding movement just like kinesin or dynein in the presence of 2 mM ATP or 2 mM GTP. We observed the molecular structure of dynamin with low-angle rotary shadowing technique and revealed that the dynamin molecule is globular in shape. Gel filtration assay revealed that these globules were the oligomers of 100-kDa dynamin polypeptide. Dynamin bound to microtubules with a 1:1 approximately 1.2 molar ratio in the absence of GTP. Quick-freeze deep-etch electron microscopy of the dynamin-microtubule complex showed that dynamin decorates the surface of microtubules helically, like a screw bolt, very orderly and tightly with 11.4 +/- 0.9 (SD)nm period. Contrary to the previous report, microtubules make bundles by the attachment of the dynamin helixes around each adjacent microtubule, and no cross-bridge formation was observed.

Indexed as

Amino Acid SequenceAnimalsBrain ChemistryCa(2+) Mg(2+)-ATPaseDynaminsFreeze EtchingGTP PhosphohydrolasesGuanine NucleotidesIn Vitro TechniquesKineticsMicroscopy, ElectronMicrotubulesMolecular Sequence DataMolecular StructureProtein ConformationRatsCa(2+) Mg(2+)-ATPaseDynaminsGTP PhosphohydrolasesGuanine Nucleotides

Identifiers

PMID1421574
PMCPMC275681
OpenAlexW2027670444

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.