Evidence map›Paper›PMID 22814378›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

Petra Van Damme, Marta Lasa, Bogdan Polevoda, Cristina Gazquez, Alberto Elosegui-Artola, Duk Soo Kim, Elena De Juan-Pardo, Kimberly Demeyer, Kristine Hole, Esther Larrea and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
–field-weighted citation impact, top 96% 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

121 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
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  19. PPARα Agonism Enhances Immune Response to Radiotherapy While Dietary Oleic Acid Results in Counteraction.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Article
  20. Article

61 more citing papers are in PubMed but not listed here.

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

16 authors at 7 institutions in 4 countries.

Petra Van DammeDepartment of Medical Protein Research, Vlaams Instituut voor Biotechnologie, Ghent University, B-9000 Ghent, Belgium. Petra.VanDamme@vib-ugent.be
Marta Lasa
Bogdan Polevoda
Cristina Gazquez
Alberto Elosegui-Artola
Duk Soo Kim
Elena De Juan-Pardo
Kimberly Demeyer
Kristine Hole
Esther Larrea
Evy Timmerman
Jesus Prieto
Thomas Arnesen
Fred Sherman
Kris Gevaert
Rafael Aldabe
University of Rochester Medical Center · USVlaams Instituut voor Biotechnologie · BECentro de Estudios e Investigaciones Técnicas de Gipuzkoa · ESCentro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas · ESGhent University · BEHaukeland University Hospital · NOUniversity of Bergen · NO

Funding

Regulation and Gene Expression of Yeast Cytochrome cR01GM012702 · NIGMS · UNIVERSITY OF ROCHESTER · PI SHERMAN, FRED · 1985 to 2010
$4.3M
NIGMS NIH HHS R01 GM012702NIGMS NIH HHS R01GM12702
6 · The paper itself

Abstract

Protein N-terminal acetylation (Nt-acetylation) is an important mediator of protein function, stability, sorting, and localization. Although the responsible enzymes are thought to be fairly well characterized, the lack of identified in vivo substrates, the occurrence of Nt-acetylation substrates displaying yet uncharacterized N-terminal acetyltransferase (NAT) specificities, and emerging evidence of posttranslational Nt-acetylation, necessitate the use of genetic models and quantitative proteomics. NatB, which targets Met-Glu-, Met-Asp-, and Met-Asn-starting protein N termini, is presumed to Nt-acetylate 15% of all yeast and 18% of all human proteins. We here report on the evolutionary traits of NatB from yeast to human and demonstrate that ectopically expressed hNatB in a yNatB-Δ yeast strain partially complements the natB-Δ phenotypes and partially restores the yNatB Nt-acetylome. Overall, combining quantitative N-terminomics with yeast studies and knockdown of hNatB in human cell lines, led to the unambiguous identification of 180 human and 110 yeast NatB substrates. Interestingly, these substrates included Met-Gln- N-termini, which are thus now classified as in vivo NatB substrates. We also demonstrate the requirement of hNatB activity for maintaining the structure and function of actomyosin fibers and for proper cellular migration. In addition, expression of tropomyosin-1 restored the altered focal adhesions and cellular migration defects observed in hNatB-depleted HeLa cells, indicative for the conserved link between NatB, tropomyosin, and actin cable function from yeast to human.

Indexed as

AcetylationAcetyltransferasesActomyosinCell LineCell MovementGenetic Complementation TestHeLa CellsHumansProtein Structure, TertiaryProteomicsSaccharomyces cerevisiaeSubstrate SpecificityTropomyosinAcetyltransferasesActomyosinTPM1 protein, humanTropomyosin

Identifiers

PMID22814378
PMCPMC3412031
OpenAlexW1568015254

What OpenQuestion holds

Textmetadata
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.