Evidence map›Paper›PMID 9874785›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Nuclear endpoint of Wnt signaling: neoplastic transformation induced by transactivating lymphoid-enhancing factor 1.

M Aoki, A Hecht, U Kruse, R Kemler, P K Vogt

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 172 citations in OpenAlex.

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  17. SUMOylation regulates the intracellular fate of ZO-2.Cellular and molecular life sciences : CMLS · 2017
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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

5 authors at 1 institution in 1 country.

M AokiDepartment of Molecular and Experimental Medicine, The Scripps Research Institute, 10550 North Torrey Pines Road, BCC-239, La Jolla, CA 92037, USA.
A Hecht
U Kruse
R Kemler
P K Vogt
Scripps Research Institute · US

Funding

P3K, RETROVIRAL ONCOGENE AND HOMOLOG OF PI 3-KINASER01CA078230 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI VOGT, PETER K · 1998 to 2013
$5.6M
ONCOGENES IN VIRUS AND CELLR35CA042564 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI VOGT, PETER K · 1986 to 1999
–
NCI NIH HHS CA42564NCI NIH HHS CA78230NCI NIH HHS R01 CA078230
6 · The paper itself

Abstract

The interaction between beta-catenin and LEF-1/TCF transcription factors plays a pivotal role in the Wnt-1 signaling pathway. The level of beta-catenin is regulated by partner proteins, including glycogen synthase kinase-3beta (GSK-3beta) and the adenomatous polyposis coli (APC) tumor suppressor protein. Genetic defects in APC are responsible for a heritable predisposition to colon cancer. APC protein and GSK-3beta bind beta-catenin, retain it in the cytoplasm, and facilitate the proteolytic degradation of beta-catenin. Abrogation of this negative regulation allows beta-catenin to translocate to the nucleus and to form a transcriptional activator complex with the DNA-binding protein lymphoid-enhancing factor 1 (LEF-1). This complex is thought to be involved in tumorigenesis. Here we show that covalent linkage of LEF-1 to beta-catenin and to transcriptional activation domains derived from the estrogen receptor or the herpes simplex virus protein VP16 generates transcriptional regulators that induce oncogenic transformation of chicken embryo fibroblasts. The chimeras between LEF-1 and beta-catenin or VP16 are constitutively active, whereas fusions of LEF-1 to the estrogen receptor are regulatable by estrogen. These experiments document the oncogenicity of transactivating LEF-1 and show that the transactivation domain normally provided by beta-catenin can be replaced by heterologous activation domains. These results suggest that the transactivating function of the LEF-1/beta-catenin complex is critical for tumorigenesis and that this complex transforms cells by activating specific LEF-1 target genes.

Indexed as

Cell Transformation, NeoplasticZebrafish ProteinsAnimalsbeta CateninChick EmbryoCytoskeletal ProteinsDNA-Binding ProteinsGenes, ReporterHerpes Simplex Virus Protein Vmw65HumansLymphoid Enhancer-Binding Factor 1MiceProto-Oncogene ProteinsReceptors, EstrogenRecombinant Fusion ProteinsTrans-Activatorsbeta CateninCTNNB1 protein, humanCTNNB1 protein, mouseCytoskeletal ProteinsDNA-Binding ProteinsHerpes Simplex Virus Protein Vmw65LEF1 protein, humanLef1 protein, mouseLymphoid Enhancer-Binding Factor 1Proto-Oncogene ProteinsReceptors, EstrogenRecombinant Fusion ProteinsTrans-ActivatorsTranscription FactorsWnt1 ProteinWNT1 protein, humanWnt1 protein, mouseWnt ProteinsZebrafish Proteins

Identifiers

PMID9874785
PMCPMC15106
OpenAlexW1983883857

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.