Evidence map›Paper›PMID 16619031›Full record

ArticleThe EMBO journal2006

A CDK-catalysed regulatory phosphorylation for formation of the DNA replication complex Sld2-Dpb11.

Yon-Soo Tak, Yoshimi Tanaka, Shizuko Endo, Yoichiro Kamimura, Hiroyuki Araki

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

55 citing papers in PubMed, 109 citations in OpenAlex.

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  12. Novel insights into the mechanism of cell cycle kinases Mec1(ATR) and Tel1(ATM).Critical reviews in biochemistry and molecular biology · 2021
    Article
  13. Budding yeast relies on GScience advances · 2021
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. TOPBP1The Journal of cell biology · 2017
    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 3 institutions in 1 country.

Yon-Soo TakDivision of Microbial Genetics, National Institute of Genetics, Research Organization of Information and Systems, Mishima, Shizuoka, Japan.
Yoshimi Tanaka
Shizuko Endo
Yoichiro Kamimura
Hiroyuki Araki
Research Organization of Information and Systems · JPThe Graduate University for Advanced Studies, SOKENDAI · JPNational Institute of Genetics · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation often regulates protein-protein interactions to control biological reactions. The Sld2 and Dpb11 proteins of budding yeast form a phosphorylation-dependent complex that is essential for chromosomal DNA replication. The Sld2 protein has a cluster of 11 cyclin-dependent kinase (CDK) phosphorylation motifs (Ser/Thr-Pro), six of which match the canonical sequences Ser/Thr-Pro-X-Lys/Arg, Lys/Arg-Ser/Thr-Pro and Ser/Thr-Pro-Lys/Arg. Simultaneous alanine substitution for serine or threonine in all the canonical CDK-phosphorylation motifs severely reduces complex formation between Sld2 and Dpb11, and inhibits DNA replication. Here we show that phosphorylation of these canonical motifs does not play a direct role in complex formation, but rather regulates phosphorylation of another residue, Thr84. This constitutes a non-canonical CDK-phosphorylation motif within a 28-amino-acid sequence that is responsible, after phosphorylation, for binding of Sld2-Dpb11. We further suggest that CDK-catalysed phosphorylation of sites other than Thr84 renders Thr84 accessible to CDK. Finally, we argue that this novel mechanism sets a threshold of CDK activity for formation of the essential Sld2 to Dpb11 complex and therefore prevents premature DNA replication.

Indexed as

DNA ReplicationAmino Acid MotifsAmino Acid SequenceCatalysisCell Cycle ProteinsCyclin-Dependent KinasesMolecular Sequence DataPhosphorylationProtein Interaction MappingSaccharomyces cerevisiae ProteinsSequence DeletionThreonineCell Cycle ProteinsCyclin-Dependent KinasesDPB11 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSLD2 protein, S cerevisiaeThreonine

Identifiers

PMID16619031
PMCPMC1456926
OpenAlexW2082128798

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.