Evidence map›Paper›PMID 28739905›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Effect of ATP and regulatory light-chain phosphorylation on the polymerization of mammalian nonmuscle myosin II.

Xiong Liu, Neil Billington, Shi Shu, Shu-Hua Yu, Grzegorz Piszczek, James R Sellers, Edward D Korn

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024
    Review
  5. Article
  6. SuggestingCells · 2024
    Article
  7. Review
  8. Article
  9. Non-muscle myosin 2 at a glance.Journal of cell science · 2023
    Review
  10. Article
  11. Article
  12. Filament evanescence of myosin II and smooth muscle function.The Journal of general physiology · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  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

7 authors.

Xiong LiuLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Neil BillingtonLaboratory of Physiology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Shi ShuLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Shu-Hua YuLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Grzegorz PiszczekBiophysics Core, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
James R SellersLaboratory of Physiology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892.
Edward D KornLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892; edk@nih.gov.

Funding

Regulation Of Smooth and Nonmuscle MyosinZIAHL001786 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI SELLERS, JAMES · 2009 to 2025
$17.4M
Biophysics FacilityZICHL000338 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI PISZCZEK, GRZEGORZ · 2009 to 2025
$12.2M
6 · The paper itself

Abstract

Addition of 1 mM ATP substantially reduces the light scattering of solutions of polymerized unphosphorylated nonmuscle myosin IIs (NM2s), and this is reversed by phosphorylation of the regulatory light chain (RLC). It has been proposed that these changes result from substantial depolymerization of unphosphorylated NM2 filaments to monomers upon addition of ATP, and filament repolymerization upon RLC-phosphorylation. We now show that the differences in myosin monomer concentration of RLC-unphosphorylated and -phosphorylated recombinant mammalian NM2A, NM2B, and NM2C polymerized in the presence of ATP are much too small to explain their substantial differences in light scattering. Rather, we find that the decrease in light scattering upon addition of ATP to polymerized unphosphorylated NM2s correlates with the formation of dimers, tetramers, and hexamers, in addition to monomers, an increase in length, and decrease in width of the bare zones of RLC-unphosphorylated filaments. Both effects of ATP addition are reversed by phosphorylation of the RLC. Our data also suggest that, contrary to previous models, assembly of RLC-phosphorylated NM2s at physiological ionic strength proceeds from folded monomers to folded antiparallel dimers, tetramers, and hexamers that unfold and polymerize into antiparallel filaments. This model could explain the dynamic relocalization of NM2 filaments in vivo by dephosphorylation of RLC-phosphorylated filaments, disassembly of the dephosphorylated filaments to folded monomers, dimers, and small oligomers, followed by diffusion of these species, and reassembly of filaments at the new location following rephosphorylation of the RLC.

Indexed as

Models, MolecularProtein MultimerizationAdenosine TriphosphateAnimalsHumansMiceMyosin Heavy ChainsMyosin Type IIPhosphorylationAdenosine TriphosphateMyosin Heavy ChainsMyosin Type IIATPlight-chain phosphorylationnonmuscle myosin IIpolymerization

Identifiers

PMID28739905
PMCPMC5559010

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.