Evidence map›Paper›PMID 31970414›Full record

ArticleNucleic acids research2020

HDAC8 cooperates with SMAD3/4 complex to suppress SIRT7 and promote cell survival and migration.

Xiaolong Tang, Guo Li, Fengting Su, Yanlin Cai, Lei Shi, Yuan Meng, Zuojun Liu, Jie Sun, Ming Wang, Minxian Qian and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

56 citing papers in PubMed, 88 citations in OpenAlex.

  1. The histone deacetylase family in health and disease.Signal transduction and targeted therapy · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Histone acetylation modulators in breast cancer.Breast cancer research : BCR · 2025
    Review
  9. Article
  10. Mechanisms of HDACs in cancer development.Frontiers in immunology · 2025
    Review
  11. The dark side of SIRT7.Molecular and cellular biochemistry · 2024
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

15 authors at 3 institutions in 1 country.

Xiaolong TangShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Guo LiDepartment of Dermatology, Xiangya Hospital, Central South University, Changsha, China.
Fengting SuShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Yanlin CaiShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Lei ShiShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Yuan MengShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Zuojun LiuShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Jie SunShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Ming WangShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Minxian QianShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Zimei WangShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Xingzhi XuGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Department of Biochemistry & Molecular Biology, School of Basic Medical Sciences, Shenzhen University Health Science Center, Shenzhen 518055, China.
Yong-Xian ChengGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Department of Biochemistry & Molecular Biology, School of Basic Medical Sciences, Shenzhen University Health Science Center, Shenzhen 518055, China.
Wei-Guo ZhuGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Department of Biochemistry & Molecular Biology, School of Basic Medical Sciences, Shenzhen University Health Science Center, Shenzhen 518055, China.
Baohua LiuShenzhen Key Laboratory for Systemic Aging and Intervention, National Engineering Research Center for Biotechnology (Shenzhen), Medical Research Center, Shenzhen University, Shenzhen 518055, China.
Shenzhen University · CNShenzhen University Health Science Center · CNCentral South University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NAD+-dependent SIRT7 deacylase plays essential roles in ribosome biogenesis, stress response, genome integrity, metabolism and aging, while how it is transcriptionally regulated is still largely unclear. TGF-β signaling is highly conserved in multicellular organisms, regulating cell growth, cancer stemness, migration and invasion. Here, we demonstrate that histone deacetylase HDAC8 forms complex with SMAD3/4 heterotrimer and occupies SIRT7 promoter, wherein it deacetylates H4 and thus suppresses SIRT7 transcription. Treatment with HDAC8 inhibitor compromises TGF-β signaling via SIRT7-SMAD4 axis and consequently, inhibits lung metastasis and improves chemotherapy efficacy in breast cancer. Our data establish a regulatory feedback loop of TGF-β signaling, wherein HDAC8 as a novel cofactor of SMAD3/4 complex, transcriptionally suppresses SIRT7 via local chromatin remodeling and thus further activates TGF-β signaling. Targeting HDAC8 exhibits therapeutic potential for TGF-β signaling related diseases.

Indexed as

Cell MovementCell Line, TumorCell SurvivalChromatin Assembly and DisassemblyDrug Resistance, NeoplasmHEK293 CellsHistone DeacetylasesHumansNeoplasm MetastasisPromoter Regions, GeneticProtein BindingRepressor ProteinsSignal TransductionSirtuinsSmad3 ProteinSmad4 ProteinHDAC8 protein, humanHistone DeacetylasesRepressor ProteinsSIRT7 protein, humanSirtuinsSmad3 ProteinSMAD3 protein, humanSmad4 ProteinSMAD4 protein, humanTransforming Growth Factor beta

Identifiers

PMID31970414
PMCPMC7102950
OpenAlexW3001213098

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.