Evidence map›Paper›PMID 21984913›Full record

ArticlePloS one2011

Regulation of septin dynamics by the Saccharomyces cerevisiae lysine acetyltransferase NuA4.

Leslie Mitchell, Andrea Lau, Jean-Philippe Lambert, Hu Zhou, Ying Fong, Jean-François Couture, Daniel Figeys, Kristin Baetz

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. 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
1.7field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  3. Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024
    Article
  4. Article
  5. Article
  6. Septins, a cytoskeletal protein family, with emerging role in striated muscle.Journal of muscle research and cell motility · 2021
    Review
  7. Article
  8. Review
  9. Review
  10. The Pseudokinase Domain ofG3 (Bethesda, Md.) · 2018
    Article
  11. Article
  12. Article
  13. Review
  14. Building a KATalogue of acetyllysine targeting and function.Briefings in functional genomics · 2016
    Review
  15. Article
  16. Septin Organization and Functions in Budding Yeast.Frontiers in cell and developmental biology · 2016
    Review
  17. Article
  18. Article
  19. Septins and Generation of Asymmetries in Fungal Cells.Annual review of microbiology · 2015
    Review
  20. Review
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

8 authors at 1 institution in 1 country.

Leslie MitchellOttawa Institute of Systems Biology, Department of Biochemistry, Microbiology, and Immunology, University of Ottawa, Ottawa, Ontario, Canada.
Andrea Lau
Jean-Philippe Lambert
Hu Zhou
Ying Fong
Jean-François Couture
Daniel Figeys
Kristin Baetz
University of Ottawa · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the budding yeast Saccharomyces cerevisiae, the lysine acetyltransferase NuA4 has been linked to a host of cellular processes through the acetylation of histone and non-histone targets. To discover proteins regulated by NuA4-dependent acetylation, we performed genome-wide synthetic dosage lethal screens to identify genes whose overexpression is toxic to non-essential NuA4 deletion mutants. The resulting genetic network identified a novel link between NuA4 and septin proteins, a group of highly conserved GTP-binding proteins that function in cytokinesis. We show that acetyltransferase-deficient NuA4 mutants have defects in septin collar formation resulting in the development of elongated buds through the Swe1-dependent morphogenesis checkpoint. We have discovered multiple sites of acetylation on four of the five yeast mitotic septins, Cdc3, Cdc10, Cdc12 and Shs1, and determined that NuA4 can acetylate three of the four in vitro. In vivo we find that acetylation levels of both Shs1 and Cdc10 are reduced in a catalytically inactive esa1 mutant. Finally, we determine that cells expressing a Shs1 protein with decreased acetylation in vivo have defects in septin localization that are similar to those observed in NuA4 mutants. These findings provide the first evidence that yeast septin proteins are acetylated and that NuA4 impacts septin dynamics.

Indexed as

AcetylationGene Regulatory NetworksHistone AcetyltransferasesHistonesLysineMutant ProteinsMutationProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsTemperatureHistone AcetyltransferasesHistonesLysineMutant ProteinsNuA4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSeptins

Identifiers

PMID21984913
PMCPMC3184947
OpenAlexW2081168830

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.