Evidence map›Paper›PMID 9009269›Full record

ArticleThe EMBO journal1997

A domain of TEL conserved in a subset of ETS proteins defines a specific oligomerization interface essential to the mitogenic properties of the TEL-PDGFR beta oncoprotein.

C Jousset, C Carron, A Boureux, C T Quang, C Oury, I Dusanter-Fourt, M Charon, J Levin, O Bernard, J Ghysdael

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

79 citing papers in PubMed, 216 citations in OpenAlex.

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19 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

10 authors at 1 institution in 1 country.

C JoussetCNRS UMR 146, Institut Curie-Section de Recherche, Centre Universitaire, Orsay, France.
C Carron
A Boureux
C T Quang
C Oury
I Dusanter-Fourt
M Charon
J Levin
O Bernard
J Ghysdael
Institut Curie · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TEL is a novel member of the ETS family of transcriptional regulators which is frequently involved in human leukemias as the result of specific chromosomal translocations. We show here by co-immunoprecipitation and GST chromatography analyses that TEL and TEL-derived fusion proteins form homotypic oligomers in vitro and in vivo. Deletion mutagenesis identifies the TEL oligomerization domain as a 65 amino acid region which is conserved in a subset of the ETS proteins including ETS-1, ETS-2, FLI-1, ERG-2 and GABP alpha in vertebrates and PNTP2, YAN and ELG in Drosophila. TEL-induced oligomerization is shown to be essential for the constitutive activation of the protein kinase activity and mitogenic properties of TEL-platelet derived growth factor receptor beta (PDGFR beta), a fusion oncoprotein characteristic of the leukemic cells of chronic myelomonocytic leukemia harboring a t(5;12) chromosomal translocation. Swapping experiments in which the TEL oligomerization domain was exchanged by the homologous domains of representative vertebrate ETS proteins including ETS-1, ERG-2 and GABP alpha show that oligomerization is a specific property of the TEL amino-terminal conserved domain. These results indicate that the amino-terminal domain conserved in a subset of the ETS proteins has evolved to generate a specialized protein-protein interaction interface which is likely to be an important determinant of their specificity as transcriptional regulators.

Indexed as

Repressor ProteinsAmino Acid SequenceAnimalsBinding SitesCell DivisionConserved SequenceDNA-Binding ProteinsDrosophilaETS Translocation Variant 6 ProteinHeLa CellsHumansMolecular Sequence DataOncogene ProteinsProto-Oncogene Proteins c-etsReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorDNA-Binding ProteinsETS Translocation Variant 6 ProteinOncogene ProteinsProto-Oncogene Proteins c-etsReceptor, Platelet-Derived Growth Factor betaReceptors, Platelet-Derived Growth FactorRepressor ProteinsTranscription Factors

Identifiers

PMID9009269
PMCPMC1169615
OpenAlexW2018075615

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.