Evidence map›Paper›PMID 9716407›Full record

ArticleGenes & development1998

Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- promoting complex at mitosis.

D Patra, W G Dunphy

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing 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

61 citing papers in PubMed, 145 citations in OpenAlex.

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  18. Taming the Beast: Control of APC/CCold Spring Harbor symposia on quantitative biology · 2017
    Article
  19. Article
  20. Mechanism of APC/CCDC20 activation by mitotic phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article

1 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

D PatraDivision of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, California 91125 USA.
W G Dunphy
California Institute of Technology · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Degradation of mitotic cyclins on exit from M phase occurs by ubiquitin-mediated proteolysis. The ubiquitination of mitotic cyclins is regulated by the anaphase-promoting complex (APC) or cyclosome. Xe-p9, the Xenopus homolog of the Suc1/Cks protein, is required for some step in mitotic cyclin destruction in Xenopus egg extracts. Specifically, if p9 is removed from interphase egg extracts, these p9-depleted extracts are unable to carry out the proteolysis of cyclin B after entry into mitosis and thus remain arrested in M phase. To explore the molecular basis of this defect, we depleted p9 from extracts that had already entered M phase and thus contained an active APC. We found that ubiquitin-mediated proteolysis of cyclin B was not compromised under these circumstances, suggesting that p9 is not directly required for ubiquitination or proteolysis. Further analysis of extracts from which p9 had been removed during interphase showed that, at the beginning of mitosis, these extracts are unable to carry out the hyperphosphorylation of the Cdc27 component of the APC, which coincides with the initial activation of the APC. p9 can be found in a complex with a small fraction of the Cdc27 protein during M phase but not interphase. The phosphorylation of the Cdc27 protein (either associated with the APC or in an isolated, bacterially expressed form) by recombinant Cdc2/cyclin B is strongly enhanced by p9. Our results indicate that p9 directly regulates the phosphorylation of the APC by Cdc2/cyclin B. These studies indicate that the Suc1/Cks protein modulates substrate recognition by a cyclin-dependent kinase.

Indexed as

Schizosaccharomyces pombe ProteinsUbiquitin-Protein Ligase ComplexesXenopus ProteinsAnaphaseAnaphase-Promoting Complex-CyclosomeAnimalsApc3 Subunit, Anaphase-Promoting Complex-CyclosomeCDC2 Protein KinaseCell Cycle ProteinsCyclin BCyclinsDNA Polymerase IIIFungal ProteinsHumansInsectaLigasesAnaphase-Promoting Complex-CyclosomeApc3 Subunit, Anaphase-Promoting Complex-CyclosomeCDC27 protein, humancdc27 protein, S pombeCDC2 Protein KinaseCell Cycle ProteinsCKS2 protein, XenopusCyclin BCyclinsDNA Polymerase IIIFungal ProteinsLigasesSchizosaccharomyces pombe ProteinsSuc1 protein, S pombeUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesXenopus Proteins

Identifiers

PMID9716407
PMCPMC317096
OpenAlexW2114480956

What OpenQuestion holds

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Registered trials

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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.