Evidence map›Paper›PMID 23831025›Full record

ArticleCell reports2013

Structural basis for LMO2-driven recruitment of the SCL:E47bHLH heterodimer to hematopoietic-specific transcriptional targets.

Kamel El Omari, Sarah J Hoosdally, Kapil Tuladhar, Dimple Karia, Elisa Hall-Ponselé, Olga Platonova, Paresh Vyas, Roger Patient, Catherine Porcher, Erika J Mancini

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

44 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Article
  3. Noncoding RNA,Molecular and cellular biology · 2025
    Article
  4. Article
  5. Transcription Factor TAL1 in Erythropoiesis.Advances in experimental medicine and biology · 2024
    Review
  6. Review
  7. Review
  8. LYL1 facilitates AETFC assembly and gene activation by recruiting CARM1 in t(8;21) AML.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Review
  10. Mechanisms of Binding Specificity among bHLH Transcription Factors.International journal of molecular sciences · 2021
    Review
  11. Article
  12. Relationship between the structure and function of the transcriptional regulator E2A.Journal of biological research (Thessalonike, Greece) · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 3 institutions in 1 country.

Kamel El OmariDivision of Structural Biology, The Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK.
Sarah J Hoosdally
Kapil Tuladhar
Dimple Karia
Elisa Hall-Ponselé
Olga Platonova
Paresh Vyas
Roger Patient
Catherine Porcher
Erika J Mancini
University of Oxford · GBCentre for Human Genetics · GBMRC Weatherall Institute of Molecular Medicine · GB

Funding

Department of HealthMedical Research Council G1000729Medical Research Council MC_U137961142Medical Research Council MC_U137961146Medical Research Council MC_U137981013Medical Research Council MC_UU_12009/8Wellcome Trust 090532Wellcome Trust 090532/Z/09/Z
6 · The paper itself

Abstract

Cell fate is governed by combinatorial actions of transcriptional regulators assembling into multiprotein complexes. However, the molecular details of how these complexes form are poorly understood. One such complex, which contains the basic-helix-loop-helix heterodimer SCL:E47 and bridging proteins LMO2:LDB1, critically regulates hematopoiesis and induces T cell leukemia. Here, we report the crystal structure of (SCL:E47)bHLH:LMO2:LDB1LID bound to DNA, providing a molecular account of the network of interactions assembling this complex. This reveals an unexpected role for LMO2. Upon binding to SCL, LMO2 induces new hydrogen bonds in SCL:E47, thereby strengthening heterodimer formation. This imposes a rotation movement onto E47 that weakens the heterodimer:DNA interaction, shifting the main DNA-binding activity onto additional protein partners. Along with biochemical analyses, this illustrates, at an atomic level, how hematopoietic-specific SCL sequesters ubiquitous E47 and associated cofactors and supports SCL's reported DNA-binding-independent functions. Importantly, this work will drive the design of small molecules inhibiting leukemogenic processes.

Indexed as

Molecular Docking SimulationTranscription, GeneticAmino Acid SequenceAnimalsBinding SitesCell Line, TumorDNAHEK293 CellsHematopoiesisHumansLIM Domain ProteinsMiceMolecular Dynamics SimulationMolecular Sequence DataMutationProtein MultimerizationDNALIM Domain Proteins

Identifiers

PMID23831025
PMCPMC3714592
OpenAlexW2149780579

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.