Evidence map›Paper›PMID 27270427›Full record

ArticleOncogene2017

Tumor suppressor bromodomain-containing protein 7 cooperates with Smads to promote transforming growth factor-β responses.

Ting Liu, Meiling Zhao, Jinquan Liu, Zhou He, Ye Zhang, Han You, Jun Huang, Xia Lin, Xin-Hua Feng

Open access · greenAbstract read
In one paragraph

Article in Oncogene, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.2field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
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  9. Article
  10. Article
  11. Review
  12. Emerging Roles of BRD7 in Pathophysiology.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Article
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  17. Review
  18. 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

9 authors at 3 institutions in 2 countries.

Ting Liu *Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Meiling Zhao *Life Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Jinquan LiuLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Zhou HeLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Ye ZhangLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Han YouState Key Laboratory of Cellular Stress Biology and Innovation Center for Cell Signaling Network, College of Life Sciences, Xiamen, Fujian 361102, China.
Jun HuangLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Xia LinMichael E. DeBakey Department of Surgery and Department of Molecular & Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Xin-Hua FengLife Sciences Institute and Innovation Center for Cell Signaling Network, Zhejiang University, Hangzhou, Zhejiang 310058, China.
Zhejiang University · CNBaylor College of Medicine · USCenter for Excellence in Molecular Cell Science · CN

Funding

Regulation of TGF-beta Receptor Signaling by HSP90R01GM063773 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2001 to 2010
$2.3M
Tumor Suppressor Function of Smad4 by UbiquitinR01CA108454 · NCI · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2004 to 2010
$1.8M
Roles of Smad1 Dephosphorylation in Osteoblast DifferentiationR01AR053591 · NIAMS · BAYLOR COLLEGE OF MEDICINE · PI FENG, XIN-HUA · 2008 to 2012
$1.5M
Regulation of SMAD2 Signaling by SMP1 PhosphataseR01DK073932 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI LIN, XIA · 2005 to 2008
$1.1M
Control of SnoN Activity by SUMO modificationR21CA112939 · NCI · BAYLOR COLLEGE OF MEDICINE · PI LIN, XIA · 2005 to 2006
$340k
NCI NIH HHS R01 CA108454NCI NIH HHS R21 CA112939NIAMS NIH HHS R01 AR053591NIDDK NIH HHS R01 DK073932NIGMS NIH HHS R01 GM063773
6 · The paper itself

Abstract

Smad proteins are central mediators in the canonical transforming growth factor-β (TGF-β) signaling pathway in mammalian cells. We report here that bromodomain-containing protein 7 (BRD7) functions as a novel transcription coactivator for Smads in TGF-β signaling. BRD7 forms a TGF-β inducible complex with Smad3/4 through its N-terminal Smad-binding domain. BRD7 simultaneously binds to acetylated histones to promote Smad-chromatin association, and associates with histone acetyltransferase p300 to enhance Smad transcriptional activity. Ectopic expression of BRD7, but not its mutants defective in Smad binding, enhances TGF-β transcriptional, tumor-suppressing and epithelial-mesenchymal transition responses. Conversely, depletion of BRD7 inhibits TGF-β responses. Thus, our study provides compelling evidence for a new function of BRD7 in fine-tuning TGF-β physiological responses.

Indexed as

A549 CellsAcetylationAnimalsBinding SitesBromodomain Containing ProteinsCell LineCell ProliferationChromosomal Proteins, Non-HistoneGene Expression RegulationHEK293 CellsHistonesHumansMicep300-CBP-Associated Factorp300-CBP Transcription FactorsSmad ProteinsBRD7 protein, humanBromodomain Containing ProteinsChromosomal Proteins, Non-HistoneHistonesp300-CBP-Associated Factorp300-CBP Transcription FactorsSmad ProteinsTransforming Growth Factor beta

Identifiers

PMID27270427
PMCPMC5140778
OpenAlexW2408875255

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.