Evidence map›Paper›PMID 27881602›Full record

ArticleGenes & development2016

N-terminal acetylation promotes synaptonemal complex assembly in C. elegans.

Jinmin Gao, Consuelo Barroso, Pan Zhang, Hyun-Min Kim, Shangtong Li, Leticia Labrador, James Lightfoot, Maxim V Gerashchenko, Vyacheslav M Labunskyy, Meng-Qiu Dong and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Structure and function of the synaptonemal complex.The Journal of cell biology · 2026
    Review
  2. Article
  3. Fine mapping and prediction of a candidate gene for wrinkled rind in melon (Cucumis melo L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
    Article
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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

12 authors at 6 institutions in 3 countries.

Jinmin GaoDepartment of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Consuelo BarrosoMedical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
Pan ZhangCollege of Life Science, Beijing Normal University, Beijing 100875, China; National Institute of Biological Sciences, Beijing 102206, China.
Hyun-Min KimDepartment of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Shangtong LiCollege of Life Science, Beijing Normal University, Beijing 100875, China; National Institute of Biological Sciences, Beijing 102206, China.
Leticia LabradorMedical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
James LightfootMedical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
Maxim V GerashchenkoDivision of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA.
Vyacheslav M LabunskyyDepartment of Dermatology, Boston University School of Medicine, Boston, Massachusetts 02218, USA.
Meng-Qiu DongCollege of Life Science, Beijing Normal University, Beijing 100875, China; National Institute of Biological Sciences, Beijing 102206, China.
Enrique Martinez-PerezMedical Research Council Clinical Sciences Centre, Imperial College London, London W12 0NN, United Kingdom.
Monica P ColaiácovoDepartment of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA.
Harvard University · USImperial College London · GBNational Institute of Biological Sciences, Beijing · CNBeijing Normal University · CNBoston University · USMedical Research Council · GB

Funding

Synaptonemal Complex Assembly and Function in MeiosisR01GM072551 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Monica P Colaiacovo · 2005 to 2026
$7.5M
Molecular mechanisms of translational regulation in agingR01AG058713 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LABUNSKYY, VYACHESLAV M · 2019 to 2023
$2.9M
Endoplasmic Reticulum Thiol Redox State and Unfolded Protein Response in AgingR00AG040191 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LABUNSKYY, VYACHESLAV M · 2014 to 2016
$723k
Endoplasmic Reticulum Thiol Redox State and Unfolded Protein Response in AgingK99AG040191 · NIA · BRIGHAM AND WOMEN'S HOSPITAL · PI LABUNSKYY, VYACHESLAV M · 2012 to 2013
$262k
Biotechnology and Biological Sciences Research Council BB/D020336/1Medical Research Council MC_U120097113NIA NIH HHS K99 AG040191NIA NIH HHS R00 AG040191NIA NIH HHS R01 AG058713NIGMS NIH HHS R01 GM072551
6 · The paper itself

Abstract

N-terminal acetylation of the first two amino acids on proteins is a prevalent cotranslational modification. Despite its abundance, the biological processes associated with this modification are not well understood. Here, we mapped the pattern of protein N-terminal acetylation in Caenorhabditis elegans, uncovering a conserved set of rules for this protein modification and identifying substrates for the N-terminal acetyltransferase B (NatB) complex. We observed an enrichment for global protein N-terminal acetylation and also specifically for NatB substrates in the nucleus, supporting the importance of this modification for regulating biological functions within this cellular compartment. Peptide profiling analysis provides evidence of cross-talk between N-terminal acetylation and internal modifications in a NAT substrate-specific manner. In vivo studies indicate that N-terminal acetylation is critical for meiosis, as it regulates the assembly of the synaptonemal complex (SC), a proteinaceous structure ubiquitously present during meiosis from yeast to humans. Specifically, N-terminal acetylation of NatB substrate SYP-1, an SC structural component, is critical for SC assembly. These findings provide novel insights into the biological functions of N-terminal acetylation and its essential role during meiosis.

Indexed as

AcetylationAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell NucleusMeiosisMutationN-Terminal Acetyltransferase BNuclear ProteinsProteomeSynaptonemal ComplexCaenorhabditis elegans ProteinsN-Terminal Acetyltransferase BNuclear ProteinsProteomeSYP-1 protein, C elegansC. elegansmeiosisNatB complexN-terminal acetylationsynaptonemal complex

Identifiers

PMID27881602
PMCPMC5131780
OpenAlexW2555441067

What OpenQuestion holds

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LicenceCC BY-NC
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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.