Evidence map›Paper›PMID 29581253›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

NAA80 is actin's N-terminal acetyltransferase and regulates cytoskeleton assembly and cell motility.

Adrian Drazic, Henriette Aksnes, Michaël Marie, Malgorzata Boczkowska, Sylvia Varland, Evy Timmerman, Håvard Foyn, Nina Glomnes, Grzegorz Rebowski, Francis Impens and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
8.7field-weighted citation impact, top 1% 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

112 citing papers in PubMed, 204 citations in OpenAlex.

  1. Alterations of actin in aging.Journal of cell science · 2026
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  13. Acetylation and Deacetylation of Cytoskeleton-Associated Proteins.Results and problems in cell differentiation · 2025
    Review
  14. Article
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52 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 4 institutions in 3 countries.

Adrian DrazicDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway.
Henriette AksnesDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway.
Michaël MarieDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway.
Malgorzata BoczkowskaDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104.
Sylvia VarlandDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway.
Evy TimmermanFlanders Institute for Biotechnology-Ghent University Center for Medical Biotechnology, B-9000 Ghent, Belgium.
Håvard FoynDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway.
Nina GlomnesDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway.
Grzegorz RebowskiDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104.
Francis ImpensFlanders Institute for Biotechnology-Ghent University Center for Medical Biotechnology, B-9000 Ghent, Belgium.ORCID 0000-0003-2886-9616
Kris GevaertFlanders Institute for Biotechnology-Ghent University Center for Medical Biotechnology, B-9000 Ghent, Belgium.
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA 19104.
Thomas ArnesenDepartment of Biological Sciences, University of Bergen, N-5020 Bergen, Norway; thomas.arnesen@uib.no.ORCID 0000-0002-3005-147X
University of Bergen · NOUniversity of Pennsylvania · USVlaams Instituut voor Biotechnologie · BEHaukeland University Hospital · NO

Funding

Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
NIGMS NIH HHS R01 GM073791
6 · The paper itself

Abstract

Actin, one of the most abundant proteins in nature, participates in countless cellular functions ranging from organelle trafficking and pathogen motility to cell migration and regulation of gene transcription. Actin's cellular activities depend on the dynamic transition between its monomeric and filamentous forms, a process exquisitely regulated in cells by a large number of actin-binding and signaling proteins. Additionally, several posttranslational modifications control the cellular functions of actin, including most notably N-terminal (Nt)-acetylation, a prevalent modification throughout the animal kingdom. However, the biological role and mechanism of actin Nt-acetylation are poorly understood, and the identity of actin's N-terminal acetyltransferase (NAT) has remained a mystery. Here, we reveal that NAA80, a suggested NAT enzyme whose substrate specificity had not been characterized, is Nt-acetylating actin. We further show that actin Nt-acetylation plays crucial roles in cytoskeletal assembly in vitro and in cells. The absence of Nt-acetylation leads to significant differences in the rates of actin filament depolymerization and elongation, including elongation driven by formins, whereas filament nucleation by the Arp2/3 complex is mostly unaffected.

Indexed as

AcetylationAcetyltransferasesActin CytoskeletonActin-Related Protein 2-3 ComplexCell MovementHEK293 CellsHumansN-Terminal AcetyltransferasesPseudopodiaAcetyltransferasesActin-Related Protein 2-3 ComplexNAA80 protein, humanN-Terminal Acetyltransferasesactincell motilityNAA80NATN-terminal acetylation

Identifiers

PMID29581253
PMCPMC5924898
OpenAlexW2789605661

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.