Evidence map›Paper›PMID 38779987›Full record

ReviewThe FEBS journal2025

Structural and functional mechanisms of actin isoforms.

Sarah M Heissler, Krishna Chinthalapudi

Abstract readReview
In one paragraph

Review in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Actin cytoskeletal dynamics in hepatic myofibroblasts and fibrosis.Nature reviews. Gastroenterology & hepatology · 2026
    Review
  3. The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. Article
  5. Alterations of actin in aging.Journal of cell science · 2026
    Review
  6. Review
  7. The Baraitser-Winter Cerebrofrontofacial Syndrome Recurrent R196H Variant in Cytoplasmic β-Actin Impairs Its Cellular Polymerization and Stability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  8. Article
  9. Article
  10. Actin isoform-specific interactions revealed byProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Nonmuscle myosin 2 turnover in cells is synergistically controlled by the tail and the motor domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Veterinary world · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Glycosylation Patterns inMicroorganisms · 2025
    Article
  18. Article
  19. 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

2 authors.

Sarah M HeisslerDepartment of Physiology and Cell Biology, Dorothy M. Davis Heart & Lung Research Institute, The Ohio State University, Columbus, OH, USA.
Krishna ChinthalapudiDepartment of Physiology and Cell Biology, Dorothy M. Davis Heart & Lung Research Institute, The Ohio State University, Columbus, OH, USA.ORCID 0000-0003-3669-561X

Funding

Structure and function of nonmuscle myosinsR01GM143539 · NIGMS · OHIO STATE UNIVERSITY · PI CHINTHALAPUDI, KRISHNA · 2021 to 2025
$2.1M
Molecular Mechanisms of Myosin-3R01GM143414 · NIGMS · OHIO STATE UNIVERSITY · PI HEISSLER, SARAH · 2021 to 2025
$1.7M
NIGMS NIH HHS R01 GM143414NIGMS NIH HHS R01GM143414NIGMS NIH HHS R01 GM143539NIGMS NIH HHS R01GM143539
6 · The paper itself

Abstract

Actin is a highly conserved and fundamental protein in eukaryotes and participates in a broad spectrum of cellular functions. Cells maintain a conserved ratio of actin isoforms, with muscle and non-muscle actins representing the main actin isoforms in muscle and non-muscle cells, respectively. Actin isoforms have specific and redundant functional roles and display different biochemistries, cellular localization, and interactions with myosins and actin-binding proteins. Understanding the specific roles of actin isoforms from the structural and functional perspective is crucial for elucidating the intricacies of cytoskeletal dynamics and regulation and their implications in health and disease. Here, we review how the structure contributes to the functional mechanisms of actin isoforms with a special emphasis on the questions of how post-translational modifications and disease-linked mutations affect actin isoforms biochemistry, function, and interaction with actin-binding proteins and myosin motors.

Indexed as

ActinsAnimalsHumansMicrofilament ProteinsMyosinsProtein BindingProtein IsoformsProtein Processing, Post-TranslationalActinsMicrofilament ProteinsMyosinsProtein Isoformsactinactin‐binding proteinsactin isoformscontractilitycytoskeletonenzymologymechanobiologymutationsmyosinpost‐translational modifications

Identifiers

PMID38779987
PMCPMC11796330

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.