Evidence map›Paper›PMID 24850890›Full record

ArticleMolecular biology of the cell2014

The 14-3-3 protein Bmh1 functions in the spindle position checkpoint by breaking Bfa1 asymmetry at yeast centrosomes.

Ayse Koca Caydasi, Yagmur Micoogullari, Bahtiyar Kurtulmus, Saravanan Palani, Gislene Pereira

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. 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. Review
  2. Determination of Anaphase Duration by Time-Lapse Microscopy in Budding Yeast.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. The signalling lipid PI3,5POpen biology · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Proteome analysis ofBiochemistry and biophysics reports · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. LTE1 promotes exit from mitosis by multiple mechanisms.Molecular biology of the cell · 2016
    Article
  16. Article
  17. Article
  18. Review
  19. The centrosome and its duplication cycle.Cold Spring Harbor perspectives in biology · 2015
    Review
  20. 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

5 authors.

Ayse Koca CaydasiMolecular Biology of Centrosomes and Cilia, German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Yagmur MicoogullariMolecular Biology of Centrosomes and Cilia, German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Bahtiyar KurtulmusMolecular Biology of Centrosomes and Cilia, German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Saravanan PalaniMolecular Biology of Centrosomes and Cilia, German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany.
Gislene PereiraMolecular Biology of Centrosomes and Cilia, German Cancer Research Center, DKFZ-ZMBH Alliance, Heidelberg 69120, Germany g.pereira@dkfz.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In addition to their well-known role in microtubule organization, centrosomes function as signaling platforms and regulate cell cycle events. An important example of such a function is the spindle position checkpoint (SPOC) of budding yeast. SPOC is a surveillance mechanism that ensures alignment of the mitotic spindle along the cell polarity axis. Upon spindle misalignment, phosphorylation of the SPOC component Bfa1 by Kin4 kinase engages the SPOC by changing the centrosome localization of Bfa1 from asymmetric (one centrosome) to symmetric (both centrosomes). Here we show that, unexpectedly, Kin4 alone is unable to break Bfa1 asymmetry at yeast centrosomes. Instead, phosphorylation of Bfa1 by Kin4 creates a docking site on Bfa1 for the 14-3-3 family protein Bmh1, which in turn weakens Bfa1-centrosome association and promotes symmetric Bfa1 localization. Consistently, BMH1-null cells are SPOC deficient. Our work thus identifies Bmh1 as a new SPOC component and refines the molecular mechanism that breaks Bfa1 centrosome asymmetry upon SPOC activation.

Indexed as

14-3-3 ProteinsChromosomes, FungalCytoskeletal ProteinsM Phase Cell Cycle CheckpointsPhosphorylationProtein BindingProtein Processing, Post-TranslationalProtein Serine-Threonine KinasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle Apparatus14-3-3 ProteinsBFA1 protein, S cerevisiaeBMH1 protein, S cerevisiaeCytoskeletal ProteinsKIN4 kinase, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID24850890
PMCPMC4091827

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.