Evidence map›Paper›PMID 16945900›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments.

Xiong Liu, Shi Shu, Myoung-Soon S Hong, Rodney L Levine, Edward D Korn

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

38 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Omics Analyses ofGenes · 2022
    Article
  8. Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  9. Targeting cytoskeletal phosphorylation in cancer.Exploration of targeted anti-tumor therapy · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. American journal of physiology. Renal physiology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Regulated methionine oxidation by monooxygenases.Free radical biology & medicine · 2017
    Review
  19. Article
  20. Review
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.

Xiong LiuLaboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Shi Shu
Myoung-Soon S Hong
Rodney L Levine
Edward D Korn
National Heart Lung and Blood Institute · US

Funding

Oxidative Modification Of ProteinsZIAHL000225 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEVINE, RODNEY L. · 2009 to 2025
$35.2M
Biochemical and Biological Properties of Actins and MyosinsZIAHL000506 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI KORN, EDWARD D · 2009 to 2014
$4.4M
OXIDATION OF PROTEINSZ01HL000225 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI LEVINE, RODNEY L. · 1985 to 2008
$4.2M
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

Dictyostelium actin was shown to become phosphorylated on Tyr-53 late in the developmental cycle and when cells in the amoeboid stage are subjected to stress but the phosphorylated actin had not been purified and characterized. We have separated phosphorylated and unphosphorylated actin and shown that Tyr-53 phosphorylation substantially reduces actin's ability to inactivate DNase I, increases actin's critical concentration, and greatly reduces its rate of polymerization. Tyr-53 phosphorylation substantially, if not completely, inhibits nucleation and elongation from the pointed end of actin filaments and reduces the rate of elongation from the barbed end. Negatively stained electron microscopic images of polymerized Tyr-53-phosphorylated actin show a variable mixture of small oligomers and filaments, which are converted to more typical, long filaments upon addition of myosin subfragment 1. Tyr-53-phosphorylated and unphosphorylated actin copolymerize in vitro, and phosphorylated and unphosphorylated actin colocalize in amoebae. Tyr-53 phosphorylation does not affect the ability of filamentous actin to activate myosin ATPase.

Indexed as

Actin CytoskeletonActinsAnimalsDictyosteliumMicroscopy, ElectronPhosphorylationPolymersProtozoan ProteinsTyrosineActinsPolymersProtozoan ProteinsTyrosine

Identifiers

PMID16945900
PMCPMC1557634
OpenAlexW2080976484

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.