Evidence map›Paper›PMID 32290654›Full record

ArticleJournal of proteome research2020

Revealing Dynamic Protein Acetylation across Subcellular Compartments.

Josue Baeza, Alexis J Lawton, Jing Fan, Michael J Smallegan, Ian Lienert, Tejas Gandhi, Oliver M Bernhardt, Lukas Reiter, John M Denu

Abstract read
In one paragraph

Article in Journal of proteome research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Bacterial protein acetylation: mechanisms, functions, and methods for study.Frontiers in cellular and infection microbiology · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Catalysis by protein acetyltransferase Gcn5.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
  18. Article
  19. Review
  20. DIA-based systems biology approach unveils E3 ubiquitin ligase-dependent responses to a metabolic shift.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

9 authors.

Josue BaezaBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, 53706 Madison, Wisconsin, United States.
Alexis J LawtonBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, 53706 Madison, Wisconsin, United States.ORCID 0000-0002-1065-0846
Jing FanWisconsin Institute for Discovery, University of Wisconsin-Madison, 53715 Madison, Wisconsin, United States.
Michael J SmalleganBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, 53706 Madison, Wisconsin, United States.
Ian LienertBiognosys AG, Wagistrasse 25, CH-8952 Schlieren, Switzerland.
Tejas GandhiBiognosys AG, Wagistrasse 25, CH-8952 Schlieren, Switzerland.
Oliver M BernhardtBiognosys AG, Wagistrasse 25, CH-8952 Schlieren, Switzerland.
Lukas ReiterBiognosys AG, Wagistrasse 25, CH-8952 Schlieren, Switzerland.ORCID 0000-0001-5751-3139
John M DenuBiomolecular Chemistry Department, School of Medicine and Public Health, University of Wisconsin-Madison, 53706 Madison, Wisconsin, United States.ORCID 0000-0001-9415-0365

Funding

GRADUATE TRAINING IN MOLECULAR BIOSCIENCEST32GM007215 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI HULL, CHRISTINA M · 1985 to 2018
$22.5M
Reversible protein acetylation and sirtuin functionR01GM065386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2003 to 2022
$7.3M
NIGMS NIH HHS R01 GM065386NIGMS NIH HHS T32 GM007215
6 · The paper itself

Abstract

Protein acetylation is a widespread post-translational modification implicated in many cellular processes. Recent advances in mass spectrometry have enabled the cataloging of thousands of sites throughout the cell; however, identifying regulatory acetylation marks have proven to be a daunting task. Knowledge of the kinetics and stoichiometry of site-specific acetylation is an important factor to uncover function. Here, an improved method of quantifying acetylation stoichiometry was developed and validated, providing a detailed landscape of dynamic acetylation stoichiometry within cellular compartments. The dynamic nature of site-specific acetylation in response to serum stimulation was revealed. In two distinct human cell lines, growth factor stimulation led to site-specific, temporal acetylation changes, revealing diverse kinetic profiles that clustered into several groups. Overlap of dynamic acetylation sites among two different human cell lines suggested similar regulatory control points across major cellular pathways that include splicing, translation, and protein homeostasis. Rapid increases in acetylation on protein translational machinery suggest a positive regulatory role under progrowth conditions. Finally, higher median stoichiometry was observed in cellular compartments where active acetyltransferases are well described. Data sets can be accessed through ProteomExchange via the MassIVE repository (ProteomExchange: PXD014453; MassIVE: MSV000084029).

Indexed as

LysineProtein Processing, Post-TranslationalAcetylationAcetyltransferasesHumansMass SpectrometryProteomeAcetyltransferasesLysineProteomeacetylationacetylomedata-independent acquisitionmass spectrometryproteomestoichiometry

Identifiers

PMID32290654
PMCPMC7427125

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.