Evidence map›Paper›PMID 32284999›Full record

ArticleScience advances2020

Mechanism of actin N-terminal acetylation.

Grzegorz Rebowski, Malgorzata Boczkowska, Adrian Drazic, Rasmus Ree, Marianne Goris, Thomas Arnesen, Roberto Dominguez

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

40 citing papers in PubMed, 60 citations in OpenAlex.

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  13. Mechanisms Involved in Therapeutic Effects ofBioMed research international · 2024
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  15. Review
  16. Article
  17. Impact of Protein NLife (Basel, Switzerland) · 2023
    Review
  18. 5,8-Dimethyl-9Pharmaceuticals (Basel, Switzerland) · 2023
    Article
  19. 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

7 authors at 3 institutions in 2 countries.

Grzegorz RebowskiDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-0766-6302
Malgorzata BoczkowskaDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-1677-023X
Adrian DrazicDepartment of Biomedicine, University of Bergen, Bergen, Norway.
Rasmus ReeDepartment of Biomedicine, University of Bergen, Bergen, Norway.ORCID 0000-0002-8446-5301
Marianne GorisDepartment of Biological Sciences, University of Bergen, Bergen, Norway.ORCID 0000-0003-0175-3082
Thomas ArnesenDepartment of Biomedicine, University of Bergen, Bergen, Norway.ORCID 0000-0002-3005-147X
Roberto DominguezDepartment of Physiology, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-3186-5229
University of Bergen · NOUniversity of Pennsylvania · USHaukeland University Hospital · NO

Funding

Structural-Functional Basis of Actin Cytoskeleton DynamicsR01GM073791 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2005 to 2025
$7.0M
BAR PROTEINS LINKING MEMBRANE AND CYTOSKELETON DYNAMICSR01MH087950 · NIMH · UNIVERSITY OF PENNSYLVANIA · PI DOMINGUEZ, ROBERTO · 2010 to 2020
$4.0M
NIGMS NIH HHS R01 GM073791NIMH NIH HHS R01 MH087950
6 · The paper itself

Abstract

About 80% of human proteins are amino-terminally acetylated (Nt-acetylated) by one of seven Nt-acetyltransferases (NATs). Actin, the most abundant protein in the cytoplasm, has its own dedicated NAT, NAA80, which acts posttranslationally and affects cytoskeleton assembly and cell motility. Here, we show that NAA80 does not associate with filamentous actin in cells, and its natural substrate is the monomeric actin-profilin complex, consistent with Nt-acetylation preceding polymerization. NAA80 Nt-acetylates actin-profilin much more efficiently than actin alone, suggesting that profilin acts as a chaperone for actin Nt-acetylation. We determined crystal structures of the NAA80-actin-profilin ternary complex, representing different actin isoforms and different states of the catalytic reaction and revealing the first structure of NAT-substrate complex at atomic resolution. The structural, biochemical, and cellular analysis of mutants shows how NAA80 has evolved to specifically recognize actin among all cellular proteins while targeting all six actin isoforms, which differ the most at the amino terminus.

Indexed as

Protein DomainsAcetylationAcetyltransferasesActinsAmino Acid SequenceBinding SitesFluorescent Antibody TechniqueHumansModels, MolecularMolecular ConformationProfilinsProtein BindingProtein IsoformsProtein MultimerizationStructure-Activity RelationshipSubstrate SpecificityAcetyltransferasesActinsNAA80 protein, humanProfilinsProtein Isoforms

Identifiers

PMID32284999
PMCPMC7141826
OpenAlexW3015309216

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

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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.