Evidence map›Paper›PMID 22854598›Full record

ArticleMolecular cell2012

PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling.

Kiyohiro Ando, Jennifer L Kernan, Peter H Liu, Takaomi Sanda, Emmanuelle Logette, Jurg Tschopp, A Thomas Look, Jianlong Wang, Lisa Bouchier-Hayes, Samuel Sidi

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

62 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Moonlighting at the Poles: Non-Canonical Functions of Centrosomes.Frontiers in cell and developmental biology · 2022
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Kiyohiro AndoDepartment of Medicine, Division of Hematology and Medical Oncology, Tisch Cancer Institute, Mount Sinai School of Medicine, New York, NY 10029, USA.
Jennifer L Kernan
Peter H Liu
Takaomi Sanda
Emmanuelle Logette
Jurg Tschopp
A Thomas Look
Jianlong Wang
Lisa Bouchier-Hayes
Samuel Sidi
Icahn School of Medicine at Mount Sinai · USDana-Farber Cancer Institute · USUniversity of Lausanne · CHBaylor College of Medicine · US

Funding

Synthetic Lethal Targeting of p53 in MyelodysplasiaR01HL088664 · NHLBI · DANA-FARBER CANCER INST · PI LOOK, A. THOMAS · 2007 to 2011
$2.1M
Oct4 and epigenetic regulation of stem cell pluripotencyR01GM095942 · NIGMS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI WANG, JIANLONG · 2011 to 2015
$1.6M
NHLBI NIH HHS HL88664NHLBI NIH HHS R01 HL088664NIGMS NIH HHS GM095942NIGMS NIH HHS R01 GM095942
6 · The paper itself

Abstract

Biochemical evidence implicates the death-domain (DD) protein PIDD as a molecular switch capable of signaling cell survival or death in response to genotoxic stress. PIDD activity is determined by binding-partner selection at its DD: whereas recruitment of RIP1 triggers prosurvival NF-κB signaling, recruitment of RAIDD activates proapoptotic caspase-2 via PIDDosome formation. However, it remains unclear how interactor selection, and thus fate decision, is regulated at the PIDD platform. We show that the PIDDosome functions in the "Chk1-suppressed" apoptotic response to DNA damage, a conserved ATM/ATR-caspase-2 pathway antagonized by Chk1. In this pathway, ATM phosphorylates PIDD on Thr788 within the DD. This phosphorylation is necessary and sufficient for RAIDD binding and caspase-2 activation. Conversely, nonphosphorylatable PIDD fails to bind RAIDD or activate caspase-2, and engages prosurvival RIP1 instead. Thus, ATM phosphorylation of the PIDD DD enables a binary switch through which cells elect to survive or die upon DNA injury.

Indexed as

Signal TransductionAtaxia Telangiectasia Mutated ProteinsCaspase 2Cell Cycle ProteinsCell DeathCells, CulturedCell SurvivalCRADD Signaling Adaptor ProteinDeath Domain Receptor Signaling Adaptor ProteinsDNA-Binding ProteinsDNA DamageHEK293 CellsHeLa CellsHumansPhosphorylationProtein Serine-Threonine KinasesAtaxia Telangiectasia Mutated ProteinsATM protein, humanCaspase 2Cell Cycle ProteinsCRADD protein, humanCRADD Signaling Adaptor ProteinDeath Domain Receptor Signaling Adaptor ProteinsDNA-Binding ProteinsPIDD1 protein, humanProtein Serine-Threonine KinasesTumor Suppressor Proteins

Identifiers

PMID22854598
PMCPMC3444620
OpenAlexW1987680504

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.