Evidence map›Paper›PMID 29384244›Full record

ArticleTraffic (Copenhagen, Denmark)2018

Rapid and dynamic arginylation of the leading edge β-actin is required for cell migration.

Iuliia Pavlyk, Nicolae A Leu, Pavan Vedula, Satoshi Kurosaka, Anna Kashina

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Review
  2. Article
  3. Methods to Study Arginylation of Tubulin.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
  12. Article
  13. Assaying Intracellular Arginylation Activity Using a Fluorescent Reporter.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  14. Nucleotide- and Protein-Dependent Functions ofMolecular biology of the cell · 2022
    Article
  15. Article
  16. α-Synuclein arginylation in the human brain.Translational neurodegeneration · 2022
    Article
  17. Article
  18. R-catcher, a potent molecular tool to unveil the arginylome.Cellular and molecular life sciences : CMLS · 2021
    Article
  19. Posttranslational modifications of the cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2021
    Review
  20. Post-translational Modifications of the Protein Termini.Frontiers in cell and developmental biology · 2021
    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.

Iuliia PavlykDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania.
Nicolae A LeuDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania.
Pavan VedulaDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania.
Satoshi KurosakaDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania.
Anna KashinaDepartment of Biomedical Sciences, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania.ORCID 0000-0002-0243-6866
University of Pennsylvania · US

Funding

Regulation of cell migration by nucleotide coding sequence and arginylationR35GM122505 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Anna S Kashina · 2017 to 2026
$6.2M
Regulation of actin during cell migrationR01GM108744 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2014 to 2017
$1.4M
Molecular Mechanisms of Protein ArginylationR01GM104003 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM104003NIGMS NIH HHS R01 GM108744NIGMS NIH HHS R35 GM122505
6 · The paper itself

Abstract

β-actin plays key roles in cell migration. Our previous work demonstrated that β-actin in migratory non-muscle cells is N-terminally arginylated and that this arginylation is required for normal lamellipodia extension. Here, we examined the function of β-actin arginylation in cell migration. We found that arginylated β-actin is concentrated at the leading edge of lamellipodia and that this enrichment is abolished after serum starvation as well as in contact-inhibited cells in confluent cultures, suggesting that arginylated β-actin at the cell leading edge is coupled to active migration. Arginylated actin levels exhibit dynamic changes in response to cell stimuli, lowered after serum starvation and dramatically elevating within minutes after cell stimulation by readdition of serum or lysophosphatidic acid. These dynamic changes require active translation and are not seen in confluent contact-inhibited cell cultures. Microinjection of arginylated actin antibodies into cells severely and specifically inhibits their migration rates. Together, these data strongly suggest that arginylation of β-actin is a tightly regulated dynamic process that occurs at the leading edge of locomoting cells in response to stimuli and is integral to the signaling network that regulates cell migration.

Indexed as

Actin CytoskeletonActinsAnimalsArginineCell MovementCells, CulturedMiceProtein Processing, Post-TranslationalSignal TransductionActinsArginineactinarginylationcell migrationlamellipodia dynamicsposttranslational modifications

Identifiers

PMID29384244
PMCPMC5869130
OpenAlexW2793641861

What OpenQuestion holds

Textmetadata
LicenceTDM
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.