Evidence map›Paper›PMID 10373527›Full record

ArticleMolecular and cellular biology1999

Activating phosphorylation of the Kin28p subunit of yeast TFIIH by Cak1p.

J Kimmelman, P Kaldis, C J Hengartner, G M Laff, S S Koh, R A Young, M J Solomon

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

34 citing papers in PubMed, 49 citations in OpenAlex.

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

7 authors at 2 institutions in 1 country.

J KimmelmanDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven Connecticut 06520-8024, USA.
P Kaldis
C J Hengartner
G M Laff
S S Koh
R A Young
M J Solomon
Yale University · USMassachusetts Institute of Technology · US

Funding

BIOCHEMISTRY OF CELL CYCLE REGULATIONR01GM047830 · NIGMS · YALE UNIVERSITY · PI SOLOMON, MARK J · 1992 to 2005
$2.2M
GENETIC AND BIOCHEMICAL ANALYSIS OF YEAST RNA POLYMERASER01GM034365 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI YOUNG, RICHARD A · 1985 to 2004
$1.8M
NIGMS NIH HHS GM34365NIGMS NIH HHS GM47830NIGMS NIH HHS R01 GM034365NIGMS NIH HHS R01 GM047830
6 · The paper itself

Abstract

Cyclin-dependent kinase (CDK)-activating kinases (CAKs) carry out essential activating phosphorylations of CDKs such as Cdc2 and Cdk2. The catalytic subunit of mammalian CAK, MO15/Cdk7, also functions as a subunit of the general transcription factor TFIIH. However, these functions are split in budding yeast, where Kin28p functions as the kinase subunit of TFIIH and Cak1p functions as a CAK. We show that Kin28p, which is itself a CDK, also contains a site of activating phosphorylation on Thr-162. The kinase activity of a T162A mutant of Kin28p is reduced by approximately 75 to 80% compared to that of wild-type Kin28p. Moreover, cells containing kin28(T162A) and a conditional allele of TFB3 (the ortholog of the mammalian MAT1 protein, an assembly factor for MO15 and cyclin H) are severely compromised and display a significant further reduction in Kin28p activity. This finding provides in vivo support for the previous biochemical observation that MO15-cyclin H complexes can be activated either by activating phosphorylation of MO15 or by binding to MAT1. Finally, we show that Kin28p is no longer phosphorylated on Thr-162 following inactivation of Cak1p in vivo, that Cak1p can phosphorylate Kin28p on Thr-162 in vitro, and that this phosphorylation stimulates the CTD kinase activity of Kin28p. Thus, Kin28p joins Cdc28p, the major cell cycle Cdk in budding yeast, as a physiological Cak1p substrate. These findings indicate that although MO15 and Cak1p constitute different forms of CAK, both control the cell cycle and the phosphorylation of the C-terminal domain of the large subunit of RNA polymerase II by TFIIH.

Indexed as

Cyclin-Dependent KinasesSaccharomyces cerevisiae ProteinsTATA-Binding Protein Associated FactorsTranscription Factors, TFIITranscription Factor TFIIDAnimalsCell CycleCyclin-Dependent Kinase-Activating KinaseEnzyme ActivationPhosphorylationPoint MutationProtein Serine-Threonine KinasesRabbitsSaccharomyces cerevisiaeThreonineTranscription FactorsCyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesKin28 protein kinase, S cerevisiaeProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsTAF6 protein, S cerevisiaeTATA-Binding Protein Associated FactorsThreonineTranscription FactorsTranscription Factors, TFIITranscription Factor TFIIDTranscription Factor TFIIH

Identifiers

PMID10373527
PMCPMC84276
OpenAlexW2137778853

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.