Evidence map›Paper›PMID 15870265›Full record

ArticleMolecular and cellular biology2005

Phosphorylation by Cak1 regulates the C-terminal domain kinase Ctk1 in Saccharomyces cerevisiae.

Denis Ostapenko, Mark J Solomon

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Cyclin-dependent kinases: Masters of the eukaryotic universe.Wiley interdisciplinary reviews. RNA · 2023
    Review
  2. Structure and activation mechanism of the yeast RNA Pol II CTD kinase CTDK-1 complex.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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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

2 authors at 1 institution in 1 country.

Denis OstapenkoYale University School of Medicine, Department of Molecular Biophysics and Biochemistry, 333 Cedar Street, New Haven, CT 06520-8024, USA.
Mark J Solomon
Yale University · US

Funding

Global Analysis of Transcription Regulatory NetworksR01CA077808 · NCI · YALE UNIVERSITY · PI SNYDER, MICHAEL P. · 1997 to 2009
$6.8M
BIOCHEMISTRY OF CELL CYCLE REGULATIONR01GM047830 · NIGMS · YALE UNIVERSITY · PI SOLOMON, MARK J · 1992 to 2005
$2.2M
NCI NIH HHS CA77808NCI NIH HHS R01 CA077808NIGMS NIH HHS GM47830NIGMS NIH HHS R01 GM047830
6 · The paper itself

Abstract

Ctk1 is a Saccharomyces cerevisiae cyclin-dependent protein kinase (CDK) that assembles with Ctk2 and Ctk3 to form an active protein kinase complex, CTDK-I. CTDK-I phosphorylates Ser2 within the RNA polymerase II C-terminal domain, an activity that is required for efficient transcriptional elongation and 3' RNA processing. Ctk1 contains a conserved T loop, which undergoes activating phosphorylation in other CDKs. We show that Ctk1 is phosphorylated on Thr-338 within the T loop. Mutation of this residue abolished Ctk1 kinase activity in vitro and resulted in a cold-sensitive phenotype. As with other yeast CDKs undergoing T-loop phosphorylation, Ctk1 phosphorylation on Thr-338 was dependent on the Cak1 protein kinase. Ctk1 isolated from cak1Delta cells was unphosphorylated and exhibited low protein kinase activity. Moreover, Cak1 directly phosphorylated Ctk1 in vitro. Unlike wild-type cells, cells expressing Ctk1(T338A) delayed growth at early stationary phase, did not show the increase in Ser2 phosphorylation that normally accompanies the transition from rapid growth to stationary phase, and had compromised transcriptional activation of two stationary-phase genes, CTT1 and SPI1. Therefore, Ctk1 phosphorylation on Thr-338 is carried out by Cak1 and is required for normal gene transcription during the transition into stationary phase.

Indexed as

Amino Acid SequenceCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesEnzyme ActivationGene Expression Regulation, FungalGenes, FungalMolecular Sequence DataPhosphorylationProtein KinasesProtein Structure, TertiaryRNA, FungalRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThreonineTranscriptional ActivationCTDK-I protein complex, S cerevisiaeCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesProtein KinasesRNA, FungalRNA Polymerase IISaccharomyces cerevisiae ProteinsThreonine

Identifiers

PMID15870265
PMCPMC1087728
OpenAlexW2161373592

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.