Evidence map›Paper›PMID 36252034›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Structures and mechanisms of actin ATP hydrolysis.

Yusuke Kanematsu, Akihiro Narita, Toshiro Oda, Ryotaro Koike, Motonori Ota, Yu Takano, Kei Moritsugu, Ikuko Fujiwara, Kotaro Tanaka, Hideyuki Komatsu and 5 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Alterations of actin in aging.Journal of cell science · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Microscopic and structural observations of actin filament capping and severing by cytochalasin D.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Mechanism of phosphate release from actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

15 authors.

Yusuke KanematsuGraduate School of Information Sciences, Hiroshima City University, Hiroshima 731-3194, Japan.
Akihiro NaritaStructural Biology Research Center, Graduate School of Science, Nagoya University, Nagoya 464-8601, Japan.ORCID 0000-0003-1504-9352
Toshiro OdaFaculty of Health and Welfare, Tokai Gakuin University, Gifu 504-8511, Japan.
Ryotaro KoikeGraduate School of Informatics, Nagoya University, Nagoya 464-8601, Japan.ORCID 0000-0003-2965-6954
Motonori OtaGraduate School of Informatics, Nagoya University, Nagoya 464-8601, Japan.ORCID 0000-0001-9090-668X
Yu TakanoGraduate School of Information Sciences, Hiroshima City University, Hiroshima 731-3194, Japan.ORCID 0000-0002-4165-8672
Kei MoritsuguGraduate School of Medical Life Science, Yokohama City University, Yokohama 230-0045, Japan.ORCID 0000-0002-2470-0859
Ikuko FujiwaraGraduate School of Science, Osaka City University, Osaka 558-8585, Japan.ORCID 0000-0002-9361-636X
Kotaro TanakaStructural Biology Research Center, Graduate School of Science, Nagoya University, Nagoya 464-8601, Japan.
Hideyuki KomatsuDepartment of Bioscience and Bioinformatics, Graduate School of Computer Science and Systems Engineering, Kyushu Institute of Technology, Iizuka 820-8502, Japan.ORCID 0000-0002-6630-0036
Takayuki NagaeSynchrotron Radiation Research Center, Nagoya University, Nagoya 464-8603, Japan.ORCID 0000-0001-7016-5183
Nobuhisa WatanabeSynchrotron Radiation Research Center, Nagoya University, Nagoya 464-8603, Japan.
Mitsusada IwasaGraduate School of Informatics, Nagoya University, Nagoya 464-8601, Japan.
Yuichiro MaédaStructural Biology Research Center, Graduate School of Science, Nagoya University, Nagoya 464-8601, Japan.ORCID 0000-0002-5173-9409
Shuichi TakedaStructural Biology Research Center, Graduate School of Science, Nagoya University, Nagoya 464-8601, Japan.ORCID 0000-0003-1383-8518

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major cytoskeleton protein actin undergoes cyclic transitions between the monomeric G-form and the filamentous F-form, which drive organelle transport and cell motility. This mechanical work is driven by the ATPase activity at the catalytic site in the F-form. For deeper understanding of the actin cellular functions, the reaction mechanism must be elucidated. Here, we show that a single actin molecule is trapped in the F-form by fragmin domain-1 binding and present their crystal structures in the ATP analog-, ADP-Pi-, and ADP-bound forms, at 1.15-Å resolutions. The G-to-F conformational transition shifts the side chains of Gln137 and His161, which relocate four water molecules including W1 (attacking water) and W2 (helping water) to facilitate the hydrolysis. By applying quantum mechanics/molecular mechanics calculations to the structures, we have revealed a consistent and comprehensive reaction path of ATP hydrolysis by the F-form actin. The reaction path consists of four steps: 1) W1 and W2 rotations; 2) P

Indexed as

ActinsProtonsAdenosine DiphosphateAdenosine TriphosphateDalteparinHydrolysisMyosinsWaterActinsAdenosine DiphosphateAdenosine TriphosphateDalteparinMyosinsProtonsWateractinATP hydrolysisprotein crystallographyQM/MM simulation

Identifiers

PMID36252034
PMCPMC9618068

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.