Evidence map›Paper›PMID 25613376›Full record

ArticleCell death and differentiation2015

TSPYL2 is an essential component of the REST/NRSF transcriptional complex for TGFβ signaling activation.

M T Epping, A Lunardi, D Nachmani, M Castillo-Martin, T H Thin, C Cordon-Cardo, P P Pandolfi

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.4field-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

29 citing papers in PubMed, 40 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. TSPYL1 as a Critical Regulator of TGFβ Signaling through Repression of TGFBR1 and TSPYL2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
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  13. Article
  14. Review
  15. LowBioMed research international · 2021
    Article
  16. Review
  17. Y chromosome in health and diseases.Cell & bioscience · 2020
    Review
  18. Review
  19. Article
  20. Article
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

7 authors at 2 institutions in 1 country.

M T EppingCancer Research Institute, Beth Israel Deaconess Cancer Center, Department of Medicine and Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
A LunardiCancer Research Institute, Beth Israel Deaconess Cancer Center, Department of Medicine and Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
D NachmaniCancer Research Institute, Beth Israel Deaconess Cancer Center, Department of Medicine and Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
M Castillo-MartinDepartment of Pathology, Mount Sinai School of Medicine, New York, NY, USA.
T H ThinDepartment of Pathology, Mount Sinai School of Medicine, New York, NY, USA.
C Cordon-CardoDepartment of Pathology, Mount Sinai School of Medicine, New York, NY, USA.
P P PandolfiCancer Research Institute, Beth Israel Deaconess Cancer Center, Department of Medicine and Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA.
Beth Israel Deaconess Medical Center · USIcahn School of Medicine at Mount Sinai · US

Funding

Scientific ReagentsP01CA087497 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI PRIVES, CAROL · 2000 to 2021
$35.4M
Targeting Tumor Suppressor Phosphatases For Cancer TherapyU01CA141496 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI PANDOLFI, PIER PAOLO · 2009 to 2013
$4.2M
NCI NIH HHS P01 CA087497NCI NIH HHS U01 CA141496NCI NIH HHS U01 CA 141496-04
6 · The paper itself

Abstract

REST/NRSF is a transcriptional repressor of neuronal genes that has been implicated in development and cancer. In epithelial tissues, REST acts as a tumor suppressor and in breast cancer, loss of REST is associated with disease recurrence and poor prognosis. Here, we identify TSPYL2 (also known as CDA1 and DENTT) as a novel component of the REST protein complex. We show that REST and TSPYL2 are regulators of TGFβ signaling and that cell-cycle arrest induced by TGFβ requires both REST and TSPYL2. Importantly, knockdown of REST or TSPYL2 resulted in transformation of human mammary epithelial cells. Mechanistically, we demonstrate that the TSPYL2/REST complex promotes TGFβ signaling by repressing the expression of genes, such as the proto-oncogene neurotrophic tyrosine kinase receptor C (TrkC). These data provide insight into the role of REST as a tumor suppressor in epithelial tissues through the regulation of the TGFβ pathway.

Indexed as

Blotting, WesternCell Line, TumorChromatin ImmunoprecipitationDNA-Binding ProteinsHumansMass SpectrometryNuclear ProteinsProto-Oncogene MasRE1-Silencing Transcription FactorRepressor ProteinsReverse Transcriptase Polymerase Chain ReactionSignal TransductionTransforming Growth Factor betaDNA-Binding ProteinsMAS1 protein, humanNuclear ProteinsProto-Oncogene MasRE1-Silencing Transcription FactorRepressor ProteinsTransforming Growth Factor betaTSPYL2 protein, human

Identifiers

PMID25613376
PMCPMC4495358
OpenAlexW1976934690

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.