Evidence map›Paper›PMID 12748387›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Dictyostelium and Acanthamoeba myosin II assembly domains go to the cleavage furrow of Dictyostelium myosin II-null cells.

Shi Shu, Xiong Liu, Edward D Korn

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Temperature dependence of myosin-II tail fragment assembly.Journal of muscle research and cell motility · 2008
    Article
  7. Article
  8. Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  9. Article
  10. Distinct pathways control recruitment and maintenance of myosin II at the cleavage furrow during cytokinesis.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  11. Article
  12. Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  13. 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.

Shi ShuLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, USA.
Xiong Liu
Edward D Korn
National Heart Lung and Blood Institute · US

Funding

Biochemical and Biological Properties of Actins and MyosinsZIAHL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 2009 to 2014
$4.4M
REGULATION OF MYOSINS AND MYOSIN KINASES (PAKs)Z01HL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 1985 to 2008
$3.7M
6 · The paper itself

Abstract

How myosin II localizes to the cleavage furrow of dividing cells is largely unknown. We show here that a 283-residue protein, assembly domain (AD)1, corresponding to the AD in the tail of Dictyostelium myosin II assembles into bundles of long tubules when expressed in myosin II-null cells and localizes to the cleavage furrow of dividing cells. AD1 mutants that do not polymerize in vitro do not go to the cleavage furrow in vivo. An assembly-competent polypeptide corresponding to the C-terminal 256 residues of Acanthamoeba myosin II also goes to the cleavage furrow of Dictyostelium myosin II-null cells. When overexpressed in wild-type cells, AD1 colocalizes with endogenous myosin II (possibly as a copolymer) in interphase, motile, and dividing cells and under caps of Con A receptors but has no effect on myosin II-dependent functions. These results suggest that neither a specific sequence, other than that required for polymerization, nor interaction with other proteins is required for localization of myosin II to the cleavage furrow.

Indexed as

AcanthamoebaAmino Acid SequenceAnimalsDictyosteliumFluorescent Antibody TechniqueMicroscopy, ElectronMutationMyosin Type IIMyosin Type II

Identifiers

PMID12748387
PMCPMC164475
OpenAlexW2009671621

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.