Evidence map›Paper›PMID 10323869›Full record

ArticleGenes & development1999

Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets.

P Kaiser, V Moncollin, D J Clarke, M H Watson, B L Bertolaet, S I Reed, E Bailly

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. State of the APC/C: organization, function, and structure.Critical reviews in biochemistry and molecular biology · 2011
    Review
  7. Article
  8. Structure characterization of the 26S proteasome.Biochimica et biophysica acta · 2011
    Review
  9. Article
  10. Article
  11. Article
  12. Loss of cks1 homeostasis deregulates cell division cycle.Journal of cellular and molecular medicine · 2010
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

7 authors at 1 institution in 2 countries.

P KaiserThe Scripps Research Institute, MB7, La Jolla, California 92037, USA.
V Moncollin
D J Clarke
M H Watson
B L Bertolaet
S I Reed
E Bailly
Scripps Research Institute · US

Funding

NIGMS NIH HHS GM38528
6 · The paper itself

Abstract

Cell cycle-specific proteolysis is critical for proper execution of mitosis in all eukaryotes. Ubiquitination and subsequent proteolysis of the mitotic regulators Clb2 and Pds1 depend on the cyclosome/APC and the 26S proteasome. We report here that components of the cell cycle machinery in yeast, specifically the cell cycle regulatory cyclin-dependent kinase Cdc28 and a conserved associated protein Cks1/Suc1, interact genetically, physically, and functionally with components of the 26S proteasome. A mutation in Cdc28 (cdc28-1N) that interferes with Cks1 binding, or inactivation of Cks1 itself, confers stabilization of Clb2, the principal mitotic B-type cyclin in budding yeast. Surprisingly, Clb2-ubiquitination in vivo and in vitro is not affected by mutations in cks1, indicating that Cks1 is not essential for cyclosome/APC activity. However, mutant Cks1 proteins no longer physically interact with the proteasome, suggesting that Cks1 is required for some aspect of proteasome function during M-phase-specific proteolysis. We further provide evidence that Cks1 function is required for degradation of the anaphase inhibitor Pds1. Stabilization of Pds1 is partially responsible for the metaphase arrest phenotype of cks1 mutants because deletion of PDS1 partially relieves the metaphase block in these mutants.

Indexed as

Cell Cycle ProteinsCyclin BSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsUbiquitin-Protein Ligase ComplexesAdaptor Proteins, Signal TransducingAnaphase-Promoting Complex-CyclosomeBase SequenceCDC28 Protein Kinase, S cerevisiaeCyclin-Dependent KinasesCyclinsCysteine EndopeptidasesDNA PrimersEndopeptidasesEnhancer Elements, GeneticFungal ProteinsAdaptor Proteins, Signal TransducingAnaphase-Promoting Complex-CyclosomeCDC28 Protein Kinase, S cerevisiaeCell Cycle ProteinsCKS1 protein, S cerevisiaeCLB2 protein, S cerevisiaeCyclin BCyclin-Dependent KinasesCyclinsCysteine EndopeptidasesDNA PrimersEndopeptidasesFungal ProteinsLigasesMultienzyme ComplexesNuclear ProteinsPDS1 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsSecurinSuc1 protein, S pombeUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesUbiquitins

Identifiers

PMID10323869
PMCPMC316943
OpenAlexW2117767151

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.