Evidence map›Paper›PMID 15601848›Full record

ArticleMolecular and cellular biology2005

Cyclin-dependent kinase activity is required for progesterone receptor function: novel role for cyclin A/Cdk2 as a progesterone receptor coactivator.

Ramesh Narayanan, Abayomi A Adigun, Dean P Edwards, Nancy L Weigel

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 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

68 citing papers in PubMed, 108 citations in OpenAlex.

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  10. Thyroid hormone receptor phosphorylation regulates acute fasting-induced suppression of the hypothalamic-pituitary-thyroid axis.Proceedings of the National Academy of Sciences of the United States of America · 2021
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8 more citing papers are in PubMed but not listed here.

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

4 authors at 3 institutions in 1 country.

Ramesh NarayananDepartment of Molecular and Cellular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Abayomi A Adigun
Dean P Edwards
Nancy L Weigel
University of Colorado Denver · USBaylor College of Medicine · USUniversity of Colorado Hospital · US

Funding

REPRODUCTIVE BIOLOGY: REGULATORY MECHANISMST32HD007165 · NICHD · BAYLOR COLLEGE OF MEDICINE · PI O'MALLEY, BERT W · 1985 to 2015
$5.6M
REGULATION OF HUMAN STEROID RECEPTORS BY PHOSPHORYLATIONR01CA057539 · NCI · BAYLOR COLLEGE OF MEDICINE · PI WEIGEL, NANCY L. · 1993 to 2010
$4.0M
NCI NIH HHS R01 CA057539NCI NIH HHS R01 CA 57539NICHD NIH HHS T32 HD007165NICHD NIH HHS T32 HD 07165
6 · The paper itself

Abstract

Our studies examining the role of the cell cycle-regulated kinase cyclin A/Cdk2 in progesterone receptor (PR) action have demonstrated that cyclin-dependent kinase activity is required for PR function and that cyclin A/Cdk2 functions as a PR coactivator. Although Cdk2 can phosphorylate PR, elimination of these phosphorylation sites has little effect on the ability of cyclin A/Cdk2 to stimulate PR activity. PR interacts with cyclin A and recruits cyclin A/Cdk2 to progestin-responsive promoters, stimulating transcription. Inhibition of Cdk2 activity abolishes progesterone-dependent activation of PR target genes in part through inhibition of PR-dependent recruitment of steroid receptor coactivator 1 (SRC-1) and subsequent histone H4 acetylation at the target promoter. In vitro studies revealed that the interaction between SRC-1 and PR is dependent upon phosphorylation of SRC-1. This heretofore-unknown mechanism provides a potential means for integrating the regulation of PR activity with cell cycle progression. Moreover, the ability of PR to recruit cyclin A/Cdk2 to target promoters provides locally elevated levels of kinase, which can preferentially facilitate phosphorylation-dependent interactions and enzymatic activities of coactivators at the target promoter.

Indexed as

AcetylationAnimalsBlotting, WesternCDC2-CDC28 KinasesCell CycleCell LineChromatin ImmunoprecipitationCOS CellsCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent KinasesGenes, ReporterGenetic VectorsGlutathione TransferaseHeLa CellsHistone AcetyltransferasesCDC2-CDC28 KinasesCDK2 protein, humanCyclin ACyclin-Dependent Kinase 2Cyclin-Dependent KinasesGlutathione TransferaseHistone AcetyltransferasesHistonesLysineNCOA1 protein, humanNuclear Receptor Coactivator 1Protein Kinase InhibitorsPurinesReceptors, ProgesteroneRoscovitineTranscription Factors

Identifiers

PMID15601848
PMCPMC538783
OpenAlexW2153687408

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.