Evidence map›Paper›PMID 8670824›Full record

ArticleThe EMBO journal1996

DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis.

Q Song, S P Lees-Miller, S Kumar, Z Zhang, D W Chan, G C Smith, S P Jackson, E S Alnemri, G Litwack, K K Khanna and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
22.0field-weighted citation impact, top 1% 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

90 citing papers in PubMed, 346 citations in OpenAlex.

  1. Secrets of DNA-PKcs beyond DNA repair.NPJ precision oncology · 2024
    Review
  2. Article
  3. Article
  4. Article
  5. Vorinostat, a pan-HDAC inhibitor, abrogates productive HPV-18 DNA amplification.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Article
  7. Proteasome inhibitor bortezomib is a novel therapeutic agent for focal radiation-induced osteoporosis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  8. Review
  9. Review
  10. Article
  11. RNF144A, an E3 ubiquitin ligase for DNA-PKcs, promotes apoptosis during DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

30 more citing papers are in PubMed but not listed here.

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

11 authors at 1 institution in 1 country.

Q SongQueensland Cancer Fund Research Unit, Queensland Institute of Medical Research, Bancroft Centre, Australia.
S P Lees-Miller
S Kumar
Z Zhang
D W Chan
G C Smith
S P Jackson
E S Alnemri
G Litwack
K K Khanna
M F Lavin
QIMR Berghofer Medical Research Institute · AU

Funding

Wellcome Trust
6 · The paper itself

Abstract

Radiosensitive cell lines derived from X-ray cross complementing group 5 (XRCC5), SCID mice and a human glioma cell line lack components of the DNA-dependent protein kinase, DNA-PK, suggesting that DNA-PK plays an important role in DNA double-strand break repair. Another enzyme implicated in DNA repair, poly(ADP-ribose) polymerase, is cleaved and inactivated during apoptosis, suggesting that some DNA repair proteins may be selectively targeted for destruction during apoptosis. Here we demonstrate that DNA-PKcs, the catalytic subunit of DNA-PK, is preferentially degraded after the exposure of different cell types to a variety of agents known to cause apoptosis. However, Ku, the DNA-binding component of the enzyme, remains intact. Degradation of DNA-PKcs was accompanied by loss of DNA-PK activity. One cell line resistant to etoposide-induced apoptosis failed to show degradation of DNA-PKcs. Protease inhibitor data implicated an ICE-like protease in the cleavage of DNA-PKcs, and it was subsequently shown that the cysteine protease CPP32, but not Mch2alpha, ICE or TX, cleaved purified DNA-PKcs into three fragments of comparable size with those observed in cells undergoing apoptosis. Cleavage sites in DNA-PKcs, determined by antibody mapping and microsequencing, were shown to be the same for CPP32 cleavage and for cleavage catalyzed by extracts from cells undergoing apoptosis. These observations suggest that DNA-PKcs is a critical target for proteolysis by an ICE-like protease during apoptosis.

Indexed as

ApoptosisDNA-Binding ProteinsAnimalsAntibodiesBase SequenceCaspase 1CatalysisCell LineCysteine EndopeptidasesDNA-Activated Protein KinaseDNA PrimersEtoposideHeLa CellsHumansHydrolysisMiceAntibodiesCaspase 1Cysteine EndopeptidasesDNA-Activated Protein KinaseDNA-Binding ProteinsDNA PrimersEtoposideNuclear ProteinsPRKDC protein, humanProtein Serine-Threonine Kinases

Identifiers

PMID8670824
PMCPMC451880
OpenAlexW25687112

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.