Evidence map›Paper›PMID 26526615›Full record

ArticleFEBS letters2015

Caspase-3 cleaved p65 fragment dampens NF-κB-mediated anti-apoptotic transcription by interfering with the p65/RPS3 interaction.

Eric M Wier, Kai Fu, Andrea Hodgson, Xin Sun, Fengyi Wan

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

5 authors at 2 institutions in 1 country.

Eric M WierDepartment of Biochemistry and Molecular Biology, USA.
Kai FuDepartment of Biochemistry and Molecular Biology, USA.
Andrea HodgsonDepartment of Biochemistry and Molecular Biology, USA; W. Harry Feinstone Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21025, USA.
Xin SunDepartment of Biochemistry and Molecular Biology, USA.
Fengyi WanDepartment of Biochemistry and Molecular Biology, USA; Department of Oncology, Johns Hopkins University, Baltimore, MD 21287, USA; Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University, Baltimore, MD 21287, USA. Electronic address: fwan1@jhu.edu.
Molecular Biology Consortium · USSidney Kimmel Comprehensive Cancer Center · 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
PARylation in genotoxic stress-induced NF-kB activation Supplement for Research on Sex/Gender InfluencesR01GM111682 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WAN, FENGYI · 2015 to 2019
$2.0M
EPA EP-D-13-052NCI NIH HHS T32 CA009110NCI NIH HHS T32CA009110NIGMS NIH HHS R01 GM111682NIGMS NIH HHS R01GM111682
6 · The paper itself

Abstract

Caspase-3-mediated p65 cleavage is believed to suppress nuclear factor-kappa B (NF-κB)-mediated anti-apoptotic transactivation in cells undergoing apoptosis. However, only a small percentage of p65 is cleaved during apoptosis, not in proportion to the dramatic reduction in NF-κB transactivation. Here we show that the p65(1-97) fragment generated by Caspase-3 cleavage interferes with ribosomal protein S3 (RPS3), an NF-κB "specifier" subunit, and selectively retards the nuclear translocation of RPS3, thus dampening the RPS3/NF-κB-dependent anti-apoptotic gene expression. Our findings reveal a novel cell fate determination mechanism to ensure cells undergo programed cell death through interfering with RPS3/NF-κB-conferred anti-apoptotic transcription by the fragment from partial p65 cleavage by activated Caspase-3.

Indexed as

ApoptosisProteolysisTranscription, GeneticAnimalsCaspase 3HEK293 CellsHumansMiceModels, MolecularPeptide FragmentsProtein BindingProtein Structure, TertiaryRibosomal ProteinsTranscription Factor RelACaspase 3Peptide FragmentsRibosomal Proteinsribosomal protein S3Transcription Factor RelAApoptosisCaspase-3 cleavageFate determinationGene transcriptionNuclear factor-kappa BRibosomal protein S3

Identifiers

PMID26526615
PMCPMC4655178
OpenAlexW1893127290

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.