Evidence map›Paper›PMID 20181827›Full record

ArticleMolecular biology of the cell2010

Arginylation regulates intracellular actin polymer level by modulating actin properties and binding of capping and severing proteins.

Sougata Saha, Maureen M Mundia, Fangliang Zhang, Ryan W Demers, Farida Korobova, Tatyana Svitkina, Alex A Perieteanu, John F Dawson, Anna Kashina

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. Article
  3. Methods to Study Arginylation of Tubulin.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Assaying the Posttranslational Arginylation of Proteins in Cultured Cells.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Article
  15. Protein Arginylation: Milestones of Discovery.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Nucleotide- and Protein-Dependent Functions ofMolecular biology of the cell · 2022
    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

9 authors.

Sougata SahaDepartment of Animal Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Maureen M Mundia
Fangliang Zhang
Ryan W Demers
Farida Korobova
Tatyana Svitkina
Alex A Perieteanu
John F Dawson
Anna Kashina

Funding

Role of Protein Arginylation in Cardiovascular DevelopmentR01HL084419 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2007 to 2011
$2.2M
NHLBI NIH HHS 5R01HL084419NHLBI NIH HHS R01 HL084419
6 · The paper itself

Abstract

Actin arginylation regulates lamella formation in motile fibroblasts, but the underlying molecular mechanisms are unknown. To understand how arginylation affects the actin cytoskeleton, we investigated the biochemical properties and the structural organization of actin filaments in wild-type and arginyltransferase (Ate1) knockout cells. We found that Ate1 knockout results in a dramatic reduction of the actin polymer levels in vivo accompanied by a corresponding increase in the monomer level. Purified nonarginylated actin has altered polymerization properties, and actin filaments from Ate1 knockout cells show altered interactions with several associated proteins. Ate1 knockout cells have severe impairment of cytoskeletal organization throughout the cell. Thus, arginylation regulates the ability of actin to form filaments in the whole cell rather than preventing the collapse of preformed actin networks at the cell leading edge as proposed in our previous model. This regulation is achieved through interconnected mechanisms that involve actin polymerization per se and through binding of actin-associated proteins.

Indexed as

Actin Capping ProteinsActin CytoskeletonActinsAnimalsArginineCell LineGelsolinHumansIntracellular SpaceMiceModels, BiologicalProtein BindingProtein Structure, QuaternaryPseudopodiaActin Capping ProteinsActinsArginineGelsolin

Identifiers

PMID20181827
PMCPMC2854093

What OpenQuestion holds

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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.