Evidence map›Paper›PMID 11226158›Full record

ArticleThe EMBO journal2001

Specificity of Cdk activation in vivo by the two Caks Mcs6 and Csk1 in fission yeast.

D Hermand, T Westerling, A Pihlak, J Y Thuret, T Vallenius, M Tiainen, J Vandenhaute, G Cottarel, C Mann, T P Mäkelä

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

16 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural basis of Cdk7 activation by dual T-loop phosphorylation.bioRxiv : the preprint server for biology · 2024
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  8. Review
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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

10 authors at 1 institution in 3 countries.

D HermandHaartman Institute & Biocentrum Helsinki, University of Helsinki, 00014 Helsinki, HUCH Laboratory Diagnostics, 00029 HYKS, Finland.
T Westerling
A Pihlak
J Y Thuret
T Vallenius
M Tiainen
J Vandenhaute
G Cottarel
C Mann
T P Mäkelä
University of Namur · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activating phosphorylation of cyclin-dependent kinases (Cdks) is mediated by at least two structurally distinct types of Cdk-activating kinases (Caks): the trimeric Cdk7-cyclin H-Mat1 complex in metazoans and the single-subunit Cak1 in budding yeast. Fission yeast has both Cak types: Mcs6 is a Cdk7 ortholog and Csk1 a single-subunit kinase. Both phosphorylate Cdks in vitro and rescue a thermosensitive budding yeast CAK1 strain. However, this apparent redundancy is not observed in fission yeast in vivo. We have identified mutants that exhibit phenotypes attributable to defects in either Mcs6-activating phosphorylation or in Cdc2-activating phosphorylation. Mcs6, human Cdk7 and budding yeast Cak1 were all active as Caks for Cdc2 when expressed in fission yeast. Although Csk1 could activate Mcs6, it was unable to activate Cdc2. Biochemical experiments supported these genetic results: budding yeast Cak1 could bind and phosphorylate Cdc2 from fission yeast lysates, whereas fission yeast Csk1 could not. These results indicate that Mcs6 is the direct activator of Cdc2, and Csk1 only activates Mcs6. This demonstrates in vivo specificity in Cdk activation by Caks.

Indexed as

Schizosaccharomyces pombe ProteinsCloning, MolecularCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme ActivationGenetic Complementation TestGlutathione TransferaseHumansOpen Reading FramesPhenotypePhosphorylationProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSchizosaccharomycesSubstrate SpecificityCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesGlutathione TransferaseProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSchizosaccharomyces pombe ProteinsSck1 protein, S pombe

Identifiers

PMID11226158
PMCPMC140202
OpenAlexW2158458162

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.