Evidence map›Paper›PMID 19203584›Full record

ArticleCell2009

DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance.

Mingan Shi, Carolyn J Vivian, Kyung-Jong Lee, Chunmin Ge, Keiko Morotomi-Yano, Claudia Manzl, Florian Bock, Shigeo Sato, Chieri Tomomori-Sato, Ruihong Zhu and 8 more

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. The Golgi complex in stress and death.Frontiers in neuroscience · 2015
    Review
  9. Article
  10. Caspase functions in cell death and disease.Cold Spring Harbor perspectives in biology · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Caspases and cancer.Cell death and differentiation · 2011
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 3 institutions in 2 countries.

Mingan ShiStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Carolyn J Vivian
Kyung-Jong Lee
Chunmin Ge
Keiko Morotomi-Yano
Claudia Manzl
Florian Bock
Shigeo Sato
Chieri Tomomori-Sato
Ruihong Zhu
Jeffrey S Haug
Selene K Swanson
Michael P Washburn
David J Chen
Benjamin P C Chen
Andreas Villunger
Laurence Florens
Chunying Du
The University of Texas Southwestern Medical Center · USInnsbruck Medical University · ATStowers Institute for Medical Research · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Roles of DNA PK in DNA Double Strand Break RepairR37CA050519 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI CHEN, DAVID J · 2003 to 2011
$3.5M
Pathway Choice of DNA Double-Strand Break RepairR01CA162804 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI DAVIS, ANTHONY J · 2012 to 2021
$3.4M
ROLES OF DNA PK IN DNA DOUBLE STRAND BREAK REPAIRR01CA050519 · NCI · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI CHEN, DAVID J · 1989 to 2001
$946k
Austrian Science Fund FWF Y 212NCI NIH HHS CA50519NCI NIH HHS P01 CA092584NCI NIH HHS P01-CA92584NCI NIH HHS R01 CA050519NCI NIH HHS R01 CA162804NCI NIH HHS R37 CA050519
6 · The paper itself

Abstract

Caspase-2 is unique among all the mammalian caspases in that it is the only caspase that is present constitutively in the cell nucleus, in addition to other cellular compartments. However, the functional significance of this nuclear localization is unknown. Here we show that DNA damage induced by gamma-radiation triggers the phosphorylation of nuclear caspase-2 at the S122 site within its prodomain, leading to its cleavage and activation. This phosphorylation is carried out by the nuclear serine/threonine protein kinase DNA-PKcs and promoted by the p53-inducible death-domain-containing protein PIDD within a large nuclear protein complex consisting of DNA-PKcs, PIDD, and caspase-2, which we have named the DNA-PKcs-PIDDosome. This phosphorylation and the catalytic activity of caspase-2 are involved in the maintenance of a G2/M DNA damage checkpoint and DNA repair mediated by the nonhomologous end-joining (NHEJ) pathway. The DNA-PKcs-PIDDosome thus represents a protein complex that impacts mammalian G2/M DNA damage checkpoint and NHEJ.

Indexed as

Cell CycleAmino Acid SequenceAnimalsCarrier ProteinsCaspase 2Cell LineCysteine EndopeptidasesDeath Domain Receptor Signaling Adaptor ProteinsDNA-Activated Protein KinaseDNA DamageFibroblastsGamma RaysHumansMiceMitosisMolecular Sequence DataCarrier ProteinsCASP2 protein, humanCaspase 2Cysteine EndopeptidasesDeath Domain Receptor Signaling Adaptor ProteinsDNA-Activated Protein KinaseNuclear ProteinsPIDD1 protein, humanPRKDC protein, human

Identifiers

PMID19203584
PMCPMC5647584
OpenAlexW1984744849

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.