Evidence map›Paper›PMID 26871441›Full record

ArticlePloS one2016

Identification of Cell Cycle Dependent Interaction Partners of the Septins by Quantitative Mass Spectrometry.

Christian Renz, Silke Oeljeklaus, Sören Grinhagens, Bettina Warscheid, Nils Johnsson, Thomas Gronemeyer

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  3. Article
  4. New Insights on the Uptake and Trafficking of Coenzyme Q.Antioxidants (Basel, Switzerland) · 2023
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Caspofungin exposure alters the core septin AspB interactome of Aspergillus fumigatus.Biochemical and biophysical research communications · 2017
    Article
  12. Review
  13. Article
  14. Article
  15. Septin Organization and Functions in Budding Yeast.Frontiers in cell and developmental biology · 2016
    Review
  16. Article
  17. Septins As Modulators of Endo-Lysosomal Membrane Traffic.Frontiers in cell and developmental biology · 2016
    Review
  18. 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

6 authors at 2 institutions in 1 country.

Christian RenzUlm University, Department of Molecular Genetics and Cell Biology, Ulm, Germany.
Silke OeljeklausUniversity of Freiburg, Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, Freiburg, Germany.
Sören GrinhagensUlm University, Department of Molecular Genetics and Cell Biology, Ulm, Germany.
Bettina WarscheidUniversity of Freiburg, Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, Freiburg, Germany.
Nils JohnssonUlm University, Department of Molecular Genetics and Cell Biology, Ulm, Germany.
Thomas GronemeyerUlm University, Department of Molecular Genetics and Cell Biology, Ulm, Germany.
Universität Ulm · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The septins are a conserved family of GTP-binding proteins that, in the baker's yeast, assemble into a highly ordered array of filaments at the mother bud neck. These filaments undergo significant structural rearrangements during the cell cycle. We aimed at identifying key components that are involved in or regulate the transitions of the septins. By combining cell synchronization and quantitative affinity-purification mass-spectrometry, we performed a screen for specific interaction partners of the septins at three distinct stages of the cell cycle. A total of 83 interaction partners of the septins were assigned. Surprisingly, we detected DNA-interacting/nuclear proteins and proteins involved in ribosome biogenesis and protein synthesis predominantly present in alpha-factor arrested that do not display an assembled septin structure. Furthermore, two distinct sets of regulatory proteins that are specific for cells at S-phase with a stable septin collar or at mitosis with split septin rings were identified. Complementary methods like SPLIFF and immunoprecipitation allowed us to more exactly define the spatial and temporal characteristics of selected hits of the AP-MS screen.

Indexed as

Gene Expression Regulation, FungalBinding SitesCell CycleCell Cycle ProteinsCytoskeletonMass SpectrometryProtein BindingProtein Interaction MappingProtein IsoformsProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeptinsCell Cycle ProteinsProtein IsoformsSaccharomyces cerevisiae ProteinsSeptins

Identifiers

PMID26871441
PMCPMC4752459
OpenAlexW2258692416

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.