Evidence map›Paper›PMID 10579723›Full record

ArticleThe Journal of cell biology1999

A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.

W Liang, H M Warrick, J A Spudich

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

17 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Article
  3. SuggestingCells · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Various Themes of Myosin Regulation.Journal of molecular biology · 2016
    Review
  8. Article
  9. Article
  10. Temperature dependence of myosin-II tail fragment assembly.Journal of muscle research and cell motility · 2008
    Article
  11. Article
  12. Article
  13. Article
  14. Signaling pathways regulating Dictyostelium myosin II.Journal of muscle research and cell motility · 2002
    Review
  15. Regulation of nonmuscle myosins by heavy chain phosphorylation.Journal of muscle research and cell motility · 2001
    Review
  16. Article
  17. A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiae.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

3 authors at 1 institution in 1 country.

W LiangDepartment of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307, USA.
H M Warrick
J A Spudich
Stanford University · US

Funding

PHS HHS NIH 46551
6 · The paper itself

Abstract

Myosin II thick filament assembly in Dictyostelium is regulated by phosphorylation at three threonines in the tail region of the molecule. Converting these three threonines to aspartates (3 x Asp myosin II), which mimics the phosphorylated state, inhibits filament assembly in vitro, and 3 x Asp myosin II fails to rescue myosin II-null phenotypes. Here we report a suppressor screen of Dictyostelium myosin II-null cells containing 3 x Asp myosin II, which reveals a 21-kD region in the tail that is critical for the phosphorylation control. These data, combined with new structural evidence from electron microscopy and sequence analyses, provide evidence that thick filament assembly control involves the folding of myosin II into a bent monomer, which is unable to incorporate into thick filaments. The data are consistent with a structural model for the bent monomer in which two specific regions of the tail interact to form an antiparallel tetrameric coiled-coil structure.

Indexed as

Actin CytoskeletonAlanineAmino Acid MotifsAnimalsAspartic AcidDictyosteliumDNA, ProtozoanHydroxyquinolinesMicroscopy, ElectronModels, BiologicalMutagenesisMyosinsPeptide MappingPeptidesPhosphorylationProtein ConformationAlanineAspartic AcidDNA, ProtozoanHydroxyquinolinesMyosinsnonyl-4-hydroxyquinoline-N-oxidePeptidesProtozoan Proteins

Identifiers

PMID10579723
PMCPMC2169343
OpenAlexW2109818377

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.