Evidence map›Paper›PMID 8930895›Full record

ArticleMolecular biology of the cell1996

Interaction between yeast Cdc6 protein and B-type cyclin/Cdc28 kinases.

S Elsasser, F Lou, B Wang, J L Campbell, A Jong

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 119 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Regulating DNA replication in eukarya.Cold Spring Harbor perspectives in biology · 2013
    Review
  5. Article
  6. Chemical visualization of phosphoproteomes on membrane.Molecular & cellular proteomics : MCP · 2012
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. ATPase-dependent cooperative binding of ORC and Cdc6 to origin DNA.Nature structural & molecular biology · 2005
    Article
  15. Article
  16. Article
  17. Eukaryotic MCM proteins: beyond replication initiation.Microbiology and molecular biology reviews : MMBR · 2004
    Review
  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

5 authors at 1 institution in 1 country.

S ElsasserBraun Laboratories, California Institute of Technology, Pasadena 91125, USA.
F Lou
B Wang
J L Campbell
A Jong
California Institute of Technology · US

Funding

ENZYMATIC MECHANISMS OF DNA REPLICATIONR01GM025508 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 1985 to 2006
$2.5M
CELLULAR PROLIFERATION AND THE CDC7 PROTEIN KINASER01GM047281 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI CAMPBELL, JUDITH L · 1992 to 1995
–
YEAST CDC6 GENE CELL CYCLE PROGRESSIONR01GM048492 · NIGMS · CHILDREN'S HOSPITAL LOS ANGELES · PI JONG, AMBROSE Y · 1993 to 1996
–
NIGMS NIH HHS GM-25508NIGMS NIH HHS GM-47281NIGMS NIH HHS GM-48492
6 · The paper itself

Abstract

During purification of recombinant Cdc6 expressed in yeast, we found that Cdc6 interacts with the critical cell cycle, cyclin-dependent protein kinase Cdc28. Cdc6 and Cdc28 can be coimmunoprecipitated from extracts, Cdc6 is retained on the Cdc28-binding matrix p13-agarose, and Cdc28 is retained on an affinity column charged with bacterially produced Cdc6. Cdc6, which is a phosphoprotein in vivo, contains five Cdc28 consensus sites and is a substrate of the Cdc28 kinase in vitro. Cdc6 also inhibits Cdc28 histone H1 kinase activity. Strikingly, Cdc6 interacts preferentially with B-type cyclin/Cdc28 complexes and not Cln/Cdc28 in log-phase cells. However, Cdc6 does not associate with Cdc28 when cells are blocked at the restrictive temperature in a cdc34 mutant, a point in the cell cycle when the B-type cyclin/Cdc28 inhibitor p40Sic1 accumulates and purified p40Sic1 inhibits the Cdc6/Cdc28 interaction. Deletion of the Cdc28 interaction domain from Cdc6 yields a protein that cannot support growth. However, when overproduced, the mutant protein can support growth. Furthermore, whereas overproduction of wild-type Cdc6 leads to growth inhibition and bud hyperpolarization, overproduction of the mutant protein supports growth at normal rates with normal morphology. Thus, the interaction may have a role in the essential function of Cdc6 in initiation and in restraining mitosis until replication is complete.

Indexed as

Cyclin BSaccharomyces cerevisiae ProteinsCDC28 Protein Kinase, S cerevisiaeCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor ProteinsCyclinsFungal ProteinsMitosisRecombinant Fusion ProteinsSaccharomyces cerevisiaeCDC28 Protein Kinase, S cerevisiaeCDC6 protein, S cerevisiaeCell Cycle ProteinsCLB2 protein, S cerevisiaeCyclin BCyclin-Dependent Kinase Inhibitor ProteinsCyclinsFungal ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSIC1 protein, S cerevisiae

Identifiers

PMID8930895
PMCPMC276021
OpenAlexW1999360313

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.