Evidence map›Paper›PMID 23715268›Full record

ArticleNature communications2013

Sam68 modulates the promoter specificity of NF-κB and mediates expression of CD25 in activated T cells.

Kai Fu, Xin Sun, Wenxin Zheng, Eric M Wier, Andrea Hodgson, Dat Q Tran, Stéphane Richard, Fengyi Wan

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

43 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  6. Review
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  8. Review
  9. Transient interactions modulate the affinity of NF-κB transcription factors for DNA.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Role of Sam68 as an adaptor protein in inflammatory signaling.Cellular and molecular life sciences : CMLS · 2024
    Review
  12. Article
  13. Review
  14. Article
  15. Article
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  18. Ablation of Sam68 in adult mice increases thermogenesis and energy expenditure.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021
    Article
  19. Article
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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

8 authors at 3 institutions in 2 countries.

Kai FuDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21025, USA.
Xin Sun
Wenxin Zheng
Eric M Wier
Andrea Hodgson
Dat Q Tran
Stéphane Richard
Fengyi Wan
Johns Hopkins University · USJewish General Hospital · CAThe University of Texas Health Science Center at Houston · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Stability and potency of LAP+FOXP3+Tregs as novel cell therapy for GVHDR01HL113304 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI TRAN, DAT QUOC · 2012 to 2016
$1.9M
Novel Subunit of NF-kB Confers Gene Regulatory SpecificityR00CA137171 · NCI · JOHNS HOPKINS UNIVERSITY · PI WAN, FENGYI · 2011 to 2013
$710k
EPA EP-D-13-052NCI NIH HHS R00 CA137171NCI NIH HHS R00CA137171NCI NIH HHS T32 CA009110NCI NIH HHS T32CA009110NHLBI NIH HHS R01 HL113304
6 · The paper itself

Abstract

CD25, the alpha chain of the interleukin-2 receptor, is expressed in activated T cells and has a significant role in autoimmune disease and tumorigenesis; however, the mechanisms regulating transcription of CD25 remain elusive. Here we identify the Src-associated substrate during mitosis of 68 kDa (Sam68) as a novel non-Rel component in the nuclear factor-kappaB (NF-κB) complex that confers CD25 transcription. Our results demonstrate that Sam68 has an essential role in the induction and maintenance of CD25 in T cells. T-cell receptor engagement triggers translocation of the inhibitor of NF-κB kinase alpha (IKKα) from the cytoplasm to the nucleus, where it phosphorylates Sam68, causing complex formation with NF-κB in the nucleus. These findings reveal the important roles of KH domain-containing components and their spatial interactions with IKKs in determining the binding targets of NF-κB complexes, thus shedding novel insights into the regulatory specificity of NF-κB.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceBase SequenceBinding SitesCell NucleusDNADNA-Binding ProteinsGene Expression RegulationGene Knockdown TechniquesHEK293 CellsHumansI-kappa B KinaseInterleukin-2 Receptor alpha SubunitJurkat CellsLymphocyte ActivationMolecular Sequence DataAdaptor Proteins, Signal TransducingDNADNA-Binding ProteinsI-kappa B KinaseIL2RA protein, humanInterleukin-2 Receptor alpha SubunitKHDRBS1 protein, humanNF-kappa BReceptors, Antigen, T-CellRibosomal ProteinsRNA-Binding ProteinsRPS3 protein, humanTranscription Factor RelA

Identifiers

PMID23715268
PMCPMC3684077
OpenAlexW2032027735

What OpenQuestion holds

Textmetadata
LicenceTDM
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.