Evidence map›Paper›PMID 15340084›Full record

ArticleMolecular and cellular biology2004

Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors.

Sohail Malik, Mohamed Guermah, Chao-Xing Yuan, Weizhen Wu, Soichiro Yamamura, Robert G Roeder

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.9field-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.

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

57 citing papers in PubMed, 107 citations in OpenAlex.

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  5. Characterization ofToxins · 2023
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  9. Mediator subunit MED1 is required for E2A-PBX1-mediated oncogenic transcription and leukemic cell growth.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  13. Molecular and cellular biology · 2019
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Sohail MalikLaboratory of Biochemistry and Molecular Biology, Rockefeller University, 1230 York Ave., New York, NY 10021, USA.
Mohamed Guermah
Chao-Xing Yuan
Weizhen Wu
Soichiro Yamamura
Robert G Roeder
Rockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The TRAP/Mediator complex serves as a coactivator for many transcriptional activators, including nuclear receptors such as the thyroid hormone receptor (TR) that targets the TRAP220 subunit. The critical but selective function of TRAP220 is evidenced by the embryonic lethal phenotype of Trap220(-)(/)(-) mice and by the observation that Trap220(-)(/)(-) fibroblasts (isolated before embryonic death) are impaired in specific nuclear receptor-dependent pathways. Here we have used a biochemical and genetic approach to understand the basis of specificity in TRAP220 function. We show that Trap220(-)(/)(-) cells possess a TRAP/Mediator complex that is relatively intact and compromised in its ability to support TR-dependent, but not VP16-dependent, transcription in vitro. Transfection studies using TRAP220 mutants revealed that the N terminus of TRAP220 is necessary and sufficient for stable association with the TRAP/Mediator complex and, further, that TRAP220-dependent TR function in transfected cells requires both of the NR boxes that contain the LXXLL motif implicated in nuclear receptor binding. Similarly, an analysis of isolated TRAP/Mediator complexes with mutations in either or both of the two NR boxes confirmed a critical role for them in in vitro coactivator function. The implications of these observations are discussed in terms of our present understanding of coactivator function.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCell LineMediator Complex Subunit 1MiceMice, KnockoutMutationReceptors, Cytoplasmic and NuclearReceptors, Thyroid HormoneRecombinant ProteinsTranscription FactorsTransfectionMed1 protein, mouseMediator Complex Subunit 1Receptors, Cytoplasmic and NuclearReceptors, Thyroid HormoneRecombinant ProteinsTranscription Factors

Identifiers

PMID15340084
PMCPMC515042
OpenAlexW2112522233

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.