Evidence map›Paper›PMID 19605686›Full record

ArticleGenes & development2009

The protein phosphatase 2A functions in the spindle position checkpoint by regulating the checkpoint kinase Kin4.

Leon Y Chan, Angelika Amon

Abstract read
In one paragraph

Article in Genes & development, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. A noncanonical GTPase signaling mechanism controls exit from mitosis in budding yeast.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Article
  4. Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. PP2A Functions during Mitosis and Cytokinesis in Yeasts.International journal of molecular sciences · 2019
    Review
  12. Article
  13. Budding YeastG3 (Bethesda, Md.) · 2018
    Article
  14. Article
  15. Article
  16. LTE1 promotes exit from mitosis by multiple mechanisms.Molecular biology of the cell · 2016
    Article
  17. Article
  18. Septin-Associated Protein Kinases in the YeastFrontiers in cell and developmental biology · 2016
    Review
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors.

Leon Y ChanDavid H. Koch Institute for Integrative Cancer Research and Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Angelika Amon

Funding

Regulation of Mitosis by Proteolysis in YeastR01GM056800 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI AMON, ANGELIKA B · 2004 to 2015
$3.4M
REGULATION OF MITOSIS BY PROTEOLYSIS IN YEASTR29GM056800 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI AMON, ANGELIKA B · 1997 to 2003
$738k
Howard Hughes Medical InstituteNIGMS NIH HHS GM056800NIGMS NIH HHS R01 GM056800NIGMS NIH HHS R29 GM056800
6 · The paper itself

Abstract

In budding yeast, a surveillance mechanism known as the spindle position checkpoint (SPOC) ensures accurate genome partitioning. In the event of spindle misposition, the checkpoint delays exit from mitosis by restraining the activity of the mitotic exit network (MEN). To date, the only component of the checkpoint to be identified is the protein kinase Kin4. Furthermore, how the kinase is regulated by spindle position is not known. Here, we identify the protein phosphatase 2A (PP2A) in complex with the regulatory subunit Rts1 as a component of the SPOC. Loss of PP2A-Rts1 function abrogates the SPOC but not other mitotic checkpoints. We further show that the protein phosphatase functions upstream of Kin4, regulating the kinase's phosphorylation and localization during an unperturbed cell cycle and during SPOC activation, thus defining the phosphatase as a key regulator of SPOC function.

Indexed as

Gene Expression Regulation, FungalGenes, cdcMitosisPhosphorylationProtein KinasesProtein Phosphatase 2Protein Serine-Threonine KinasesProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusKIN4 kinase, S cerevisiaeProtein KinasesProtein Phosphatase 2Protein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID19605686
PMCPMC2714715

What OpenQuestion holds

Textmetadata
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.