Evidence map›Paper›PMID 10779356›Full record

ArticleMolecular and cellular biology2000

Distinct phosphoisoforms of the Xenopus Mcm4 protein regulate the function of the Mcm complex.

I Pereverzeva, E Whitmire, B Khan, M Coué

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. 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
1.2field-weighted citation impact, top 22% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Genomic instability in cancer.Cold Spring Harbor perspectives in biology · 2013
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
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  12. Article
  13. Review
  14. Article
  15. Geminin stabilizes Cdt1 during meiosis in Xenopus oocytes.The Journal of biological chemistry · 2009
    Article
  16. Article
  17. Article
  18. Article
  19. Eukaryotic MCM proteins: beyond replication initiation.Microbiology and molecular biology reviews : MMBR · 2004
    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

4 authors at 1 institution in 1 country.

I PereverzevaDepartment of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA.
E Whitmire
B Khan
M Coué
Texas Tech University Health Sciences Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Initiation of DNA replication in eukaryotes requires the assembly of prereplication complexes (pre-Rcs) at the origins of replication. The assembly and function of the pre-Rcs appear to be controlled by phosphorylation events. In this study we report the detailed characterization of the cell cycle phosphorylation of one component of the Xenopus pre-Rcs, the Mcm protein complex. We show that individual Mcm subunits are differentially phosphorylated during the cell cycle. During mitosis, the Mcm4 subunit is hyperphosphorylated, while the other subunits are not actively phosphorylated. The mitotic phosphorylation of Mcm4 requires Cdc2-cyclin B and other unknown kinases. Following exit from mitosis, the Mcm4 subunit of the cytosolic interphase complex undergoes dephosphorylation, and the Mcm2, Mcm3, or Mcm6 subunits are then actively phosphorylated by kinase(s) other than cyclin-dependent kinases (Cdks) or Cdc7. The association of the Mcm complex with the pre-Rcs correlates with the formation of a transient interphase complex. This complex contains an intermediately phosphorylated Mcm4 subunit and is produced by partial dephosphorylation of the mitotic hyperphosphorylated Mcm4 protein. Complete dephosphorylation of the Mcm4 subunit inactivates the Mcm complex and prevents its binding to the chromatin. Once the Mcm complex is assembled on the chromatin the Mcm4 and the Mcm2 proteins are the only subunits phosphorylated during the activation of the pre-Rcs. These chromatin-associated phosphorylations require nuclear transport and are independent of Cdk2-cyclin E. These results suggest that the changes in Mcm4 phosphorylation regulate pre-Rc assembly and the function of the pre-Rcs on the chromatin.

Indexed as

DNA-Binding ProteinsDNA ReplicationReplication OriginSaccharomyces cerevisiae ProteinsXenopus ProteinsAnimalsBiological TransportCDC2 Protein KinaseCell Cycle ProteinsCell NucleusChromatinChromosomal Proteins, Non-HistoneCyclin BInterphaseMinichromosome Maintenance Complex Component 4Minichromosome Maintenance Complex Component 6CDC2 Protein KinaseCDC7 protein, S cerevisiaeCDC7 protein, XenopusCell Cycle ProteinsChromatinChromosomal Proteins, Non-HistoneCyclin BDNA-Binding ProteinsMCM4 protein, S cerevisiaemcm6a protein, XenopusMCM6 protein, S cerevisiaeMinichromosome Maintenance Complex Component 4Minichromosome Maintenance Complex Component 6PhosphoproteinsProtein IsoformsProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsXenopus Proteins

Identifiers

PMID10779356
PMCPMC85659
OpenAlexW2157839005

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.