Evidence map›Paper›PMID 18391023›Full record

ArticleMolecular and cellular biology2008

PTEN represses RNA polymerase III-dependent transcription by targeting the TFIIIB complex.

Annette Woiwode, Sandra A S Johnson, Shuping Zhong, Cheng Zhang, Robert G Roeder, Martin Teichmann, Deborah L Johnson

Registry-linked trialOpen access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT02730923 (A Multicentric, Randomized, Non Comparative, Open-label Phase I/II Evaluating AZD2014), which is not on this map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
3.0field-weighted citation impact, top 9% 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.

NCT02730923 phase1 / phase2unknown statusnot on this mapstarted 2016, after this paper: background citation

A Multicentric, Randomized, Non Comparative, Open-label Phase I/II Evaluating AZD2014 (Dual Mammalian Target of Rapamycin Complex 1/2 (mTORC1/mTORC2) Inhibitor) in Combination With Anastrozole Versus Anastrozole Alone in the Treatment of Metastatic Hormone Receptor-positive Endometrial Adenocarcinoma

TypeinterventionalSponsorCentre Leon BerardRan2016 to 2024Enrolled72ConditionsEndometrial Carcinoma, Metastatic Carcinoma, Hormone Receptor Positive TumorArmsAZD2014, Anastrozole
3 · Its place in the literature

Who cites it

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 96 citations in OpenAlex.

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9 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

7 authors at 3 institutions in 2 countries.

Annette WoiwodeDepartment of Biochemistry and Molecular Biology, University of Southern California, Keck School of Medicine and the Norris Comprehensive Cancer Center, Los Angeles, California 90033, USA.
Sandra A S Johnson
Shuping Zhong
Cheng Zhang
Robert G Roeder
Martin Teichmann
Deborah L Johnson
University of Southern California · USInstitut Européen de Chimie et Biologie · FRRockefeller University · US

Funding

Novel targets that are deregulated by loss of PTENR01CA108614 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JOHNSON, DEBORAH L. · 2006 to 2016
$2.7M
NCI NIH HHS CA108614NCI NIH HHS R01 CA108614
6 · The paper itself

Abstract

PTEN, a tumor suppressor whose function is frequently lost in human cancers, possesses a lipid phosphatase activity that represses phosphatidylinositol 3-kinase (PI3K) signaling, controlling cell growth, proliferation, and survival. The potential for PTEN to regulate the synthesis of RNA polymerase (Pol) III transcription products, including tRNAs and 5S rRNAs, was evaluated. The expression of PTEN in PTEN-deficient cells repressed RNA Pol III transcription, whereas decreased PTEN expression enhanced transcription. Transcription repression by PTEN was uncoupled from PTEN-mediated effects on the cell cycle and was independent of p53. PTEN acts through its lipid phosphatase activity, inhibiting the PI3K/Akt/mTOR/S6K pathway to decrease transcription. PTEN, through the inactivation of mTOR, targets the TFIIIB complex, disrupting the association between TATA-binding protein and Brf1. Kinetic analysis revealed that PTEN initially induces a decrease in the serine phosphorylation of Brf1, leading to a selective reduction in the occupancy of all TFIIIB subunits on tRNA(Leu) genes, whereas prolonged PTEN expression results in the enhanced serine phosphorylation of Bdp1. Together, these results demonstrate a new class of genes regulated by PTEN through its ability to repress the activation of PI3K/Akt/mTOR/S6K signaling.

Indexed as

Gene Expression Regulation, NeoplasticCell CycleCell Line, TumorCytoplasmHumansModels, BiologicalPhosphatidate PhosphatasePhosphatidylinositol 3-KinasesPhosphorylationPTEN PhosphohydrolaseRNA Polymerase IIISignal TransductionTranscription Factor TFIIIBTranscription, GeneticTumor Suppressor Protein p53lipid phosphate phosphatasePhosphatidate PhosphatasePhosphatidylinositol 3-KinasesPTEN PhosphohydrolaseRNA Polymerase IIITranscription Factor TFIIIBTumor Suppressor Protein p53

Identifiers

PMID18391023
PMCPMC2423115
OpenAlexW1997503128

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.