Evidence map›Paper›PMID 34152688›Full record

ReviewCytoskeleton (Hoboken, N.J.)2021

Posttranslational modifications of the cytoskeleton.

Brittany MacTaggart, Anna Kashina

Open access · bronzeAbstract readReview
In one paragraph

Review in Cytoskeleton (Hoboken, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

37 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Motor-Assisted Co-Migration of Intracellular Organelles and Microtubules as a Mechanism for Directed Cargo Transport.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. The important interplay between metal ions and the intermediate filament protein vimentin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025
    Review
  12. Review
  13. Article
  14. Review
  15. Article
  16. Review
  17. Chemical Carbonylation of Arginine in Peptides and Proteins.Journal of the American Chemical Society · 2025
    Article
  18. Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Brittany MacTaggartSchool of Veterinary Medicine, Department of Biomedical Sciences, University of Pennsylvania, Philadelphia, Pennsylvania, USA.ORCID 0000-0001-7674-6042
Anna KashinaSchool of Veterinary Medicine, Department of Biomedical Sciences, University of Pennsylvania, Philadelphia, Pennsylvania, USA.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
Role of arginylation in prevention of alpha synuclein-driven neurodegenerationR01NS102435 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI KASHINA, ANNA S · 2019 to 2023
$2.6M
NIGMS NIH HHS R35 GM122505NINDS NIH HHS R01 NS102435
6 · The paper itself

Abstract

The cytoskeleton plays important roles in many essential processes at the cellular and organismal levels, including cell migration and motility, cell division, and the establishment and maintenance of cell and tissue architecture. In order to facilitate these varied functions, the main cytoskeletal components-microtubules, actin filaments, and intermediate filaments-must form highly diverse intracellular arrays in different subcellular areas and cell types. The question of how this diversity is conferred has been the focus of research for decades. One key mechanism is the addition of posttranslational modifications (PTMs) to the major cytoskeletal proteins. This posttranslational addition of various chemical groups dramatically increases the complexity of the cytoskeletal proteome and helps facilitate major global and local cytoskeletal functions. Cytoskeletal proteins undergo many PTMs, most of which are not well understood. Recent technological advances in proteomics and cell biology have allowed for the in-depth study of individual PTMs and their functions in the cytoskeleton. Here, we provide an overview of the major PTMs that occur on the main structural components of the three cytoskeletal systems-tubulin, actin, and intermediate filament proteins-and highlight the cellular function of these modifications.

Indexed as

CytoskeletonProtein Processing, Post-TranslationalCytoskeletal ProteinsIntermediate FilamentsMicrotubulesCytoskeletal Proteinsactincytoskeletonintermediate filamentsmicrotubulesposttranslational modifications

Identifiers

PMID34152688
PMCPMC8856578
OpenAlexW3176805581

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.