Evidence map›Paper›PMID 18458084›Full record

ArticleThe Journal of biological chemistry2008

Caspase-8 cleaves histone deacetylase 7 and abolishes its transcription repressor function.

Fiona L Scott, Greg J Fuchs, Sarah E Boyd, Jean-Bernard Denault, Christine J Hawkins, Franck Dequiedt, Guy S Salvesen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

25 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Role of caspase-8 in thymus function.Cell death and differentiation · 2014
    Review
  10. Proteasomal regulation of caspase-8 in cancer cell apoptosis.Apoptosis : an international journal on programmed cell death · 2013
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

7 authors at 3 institutions in 3 countries.

Fiona L ScottProgram in Apoptosis and Cell Death Research, Burnham Institute for Medical Research, La Jolla, California 92037, USA. fscott@burnham.org
Greg J Fuchs
Sarah E Boyd
Jean-Bernard Denault
Christine J Hawkins
Franck Dequiedt
Guy S Salvesen
Sanford Burnham Prebys Medical Discovery Institute · USLa Trobe University · AUMonash University · AU

Funding

CORE 6 : PROJECT LEADERSHIP AND ADMINISTRATIONU54RR020843 · NCRR · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI SMITH, JEFFREY W · 2004 to 2009
$19.1M
SPHINGOMYELIN SIGNALING PATHWAY IN FAS-INDUCED APOPTOSISP01CA069381 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI WARE, CARL F · 1996 to 2009
$16.8M
NCI NIH HHS CA69381NCRR NIH HHS RR20843
6 · The paper itself

Abstract

Caspase-8 is the initiator caspase of the extrinsic apoptosis pathway and also has a role in non-apoptotic physiologies. Identifying endogenous substrates for caspase-8 by using integrated bioinformatics and biological approaches is required to delineate the diverse roles of this caspase. We describe a number of novel putative caspase-8 substrates using the Prediction of Protease Specificity (PoPS) program, one of which is histone deacetylase 7 (HDAC7). HDAC7 is cleaved faster than any other caspase-8 substrate described to date. It is also cleaved in primary CD4+CD8+ thymocytes undergoing extrinsic apoptosis. By using naturally occurring caspase inhibitors that have evolved exquisite specificity at concentrations found within the cell, we could unequivocally assign the cleavage activity to caspase-8. Importantly, cleavage of HDAC7 alters its subcellular localization and abrogates its Nur77 repressor function. Thus we demonstrate a direct role for initiator caspase-mediated proteolysis in promoting gene transcription.

Indexed as

SoftwareAnimalsApoptosisCaspase 8Caspase InhibitorsChlorocebus aethiopsCOS CellsDNA-Binding ProteinsHistone DeacetylasesHumansMiceNuclear Receptor Subfamily 4, Group A, Member 1Protease InhibitorsReceptors, SteroidRepressor ProteinsSubstrate SpecificityCaspase 8Caspase InhibitorsDNA-Binding ProteinsHDAC7 protein, humanHdac7 protein, mouseHistone DeacetylasesNR4A1 protein, humanNr4a1 protein, mouseNuclear Receptor Subfamily 4, Group A, Member 1Protease InhibitorsReceptors, SteroidRepressor Proteins

Identifiers

PMID18458084
PMCPMC2443678
OpenAlexW1969281441

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.