Evidence map›Paper›PMID 16428435›Full record

ArticleMolecular and cellular biology2006

Cyclin-dependent kinase 9 (Cdk9) of fission yeast is activated by the CDK-activating kinase Csk1, overlaps functionally with the TFIIH-associated kinase Mcs6, and associates with the mRNA cap methyltransferase Pcm1 in vivo.

Yi Pei, Hongyan Du, Juliet Singer, Courtney Stamour, Selena Granitto, Stewart Shuman, Robert P Fisher

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.6field-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

40 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023
    Review
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  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Cap-binding complex (CBC).The Biochemical journal · 2014
    Review
  18. Article
  19. 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

7 authors at 2 institutions in 1 country.

Yi PeiMolecular Biology Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY. r-fisher@ski.mskcc.org.
Hongyan Du
Juliet Singer
Courtney Stamour
Selena Granitto
Stewart Shuman
Robert P Fisher
Rockefeller University · USMemorial Sloan Kettering Cancer Center · US

Funding

mRNA Capping EnzymesR01GM052470 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SCHWER, BEATE, SHUMAN, STEWART H · 1995 to 2019
$9.9M
The CAK Network in Metazoan Cell Cycle RegulationR01GM056985 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI FISHER, ROBERT P · 1998 to 2010
$4.3M
NIGMS NIH HHS GM52470NIGMS NIH HHS GM56985NIGMS NIH HHS R01 GM052470NIGMS NIH HHS R01 GM056985
6 · The paper itself

Abstract

Cyclin-dependent kinase 9 (Cdk9) of fission yeast is an essential ortholog of metazoan positive transcription elongation factor b (P-TEFb), which is proposed to coordinate capping and elongation of RNA polymerase II (Pol II) transcripts. Here we show that Cdk9 is activated to phosphorylate Pol II and the elongation factor Spt5 by Csk1, one of two fission yeast CDK-activating kinases (CAKs). Activation depends on Cdk9 T-loop residue Thr-212. The other CAK-Mcs6, the kinase component of transcription factor IIH (TFIIH)-cannot activate Cdk9. Consistent with the specificities of the two CAKs in vitro, the kinase activity of Cdk9 is reduced approximately 10-fold by csk1 deletion, and Cdk9 complexes from csk1Delta but not csk1+ cells can be activated by Csk1 in vitro. A cdk9(T212A) mutant is viable but phenocopies conditional growth defects of csk1Delta strains, indicating a role for Csk1-dependent activation of Cdk9 in vivo. A cdk9(T212A) mcs6(S165A) strain, in which neither Cdk9 nor Mcs6 can be activated by CAK, has a synthetic growth defect, implying functional overlap between the two CDKs, which have distinct but overlapping substrate specificities. Cdk9 forms complexes in vivo with the essential cyclin Pch1 and with Pcm1, the mRNA cap methyltransferase. The carboxyl-terminal region of Cdk9, through which it interacts with another capping enzyme, the RNA triphosphatase Pct1, is essential. Together, the data support a proposed model whereby Cdk9/Pch1-the third essential CDK-cyclin complex described in fission yeast-helps to target the capping apparatus to the transcriptional elongation complex.

Indexed as

Chromosomal Proteins, Non-HistoneCyclin-Dependent Kinase 9Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsEnzyme ActivationGene DeletionMethyltransferasesMutationPhosphorylationProtein KinasesRNA Polymerase IISchizosaccharomycesSchizosaccharomyces pombe ProteinsThreonineTranscriptional Elongation FactorsChromosomal Proteins, Non-HistoneCsk1 protein, S pombeCyclin-Dependent Kinase 9Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesCyclinsMethyltransferasesmRNA (guanine(N7))-methyltransferasePch1 protein, S pombeProtein KinasesRNA Polymerase IISchizosaccharomyces pombe ProteinsSPT5 transcriptional elongation factorThreonineTranscriptional Elongation Factors

Identifiers

PMID16428435
PMCPMC1347026
OpenAlexW2163952392

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.