Evidence map›Paper›PMID 24362031›Full record

ArticleThe Journal of biological chemistry2014

A Complex between Atg7 and Caspase-9: A NOVEL MECHANISM OF CROSS-REGULATION BETWEEN AUTOPHAGY AND APOPTOSIS.

Jie Han, Wen Hou, Leslie A Goldstein, Donna B Stolz, Simon C Watkins, Hannah Rabinowich

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed, 2 pooled it
3.9field-weighted citation impact, top 6% 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

70 citing papers in PubMed, 2 syntheses or guidelines pooled it, 100 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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  13. Review
  14. Article
  15. Review
  16. Ablation of endothelialAutophagy · 2023
    Article
  17. Article
  18. ROS-Induced DNA-Damage and Autophagy in Oral Squamous Cell Carcinoma byInternational journal of molecular sciences · 2022
    Article
  19. Review
  20. Article

10 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

6 authors at 1 institution in 1 country.

Jie HanDepartment of Pathology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15213.
Wen HouDepartment of Pathology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15213.
Leslie A GoldsteinDepartment of Pathology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15213.
Donna B StolzDepartment of Cell Biology and Physiology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15213.
Simon C WatkinsDepartment of Cell Biology and Physiology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15213.
Hannah RabinowichDepartment of Pathology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania 15213. Electronic address: rabinow@pitt.edu.
UPMC Hillman Cancer Center · US

Funding

Fluorescent Biosensors for Networks and PathwaysU54GM103529 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI WAGGONER, ALAN S. · 2012 to 2013
$6.3M
Cross-regulation of apoptosis and autophagy as a molecular basis for reversal ofR01CA134776 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI RABINOWICH, HANNAH · 2009 to 2012
$1.2M
NCI NIH HHS R01 CA134776NIGMS NIH HHS U54 GM103529
6 · The paper itself

Abstract

Several cross-talk mechanisms between autophagy and apoptosis have been identified, in which certain co-regulators are shared, allowing the same protein to participate in these opposing processes. Our studies suggest that caspase-9 is a novel co-regulator of apoptosis and autophagy and that its caspase catalytic activity is dispensable for its autophagic role. We provide evidence that caspase-9 facilitates the early events leading to autophagosome formation; that it forms a complex with Atg7; that Atg7 is not a direct substrate for caspase-9 proteolytic activity; and that, depending on the cellular context, Atg7 represses the apoptotic capability of caspase-9, whereas the latter enhances the Atg7-mediated formation of light chain 3-II. The repression of caspase-9 apoptotic activity is mediated by its direct interaction with Atg7, and it is not related to the autophagic function of Atg7. We propose that the Atg7·caspase-9 complex performs a dual function of linking caspase-9 to the autophagic process while keeping in check its apoptotic activity.

Indexed as

ApoptosisAutophagyAnimalsAutophagy-Related Protein 7Caspase 9Cell Line, TumorHumansMiceMicrotubule-Associated ProteinsMultienzyme ComplexesRNA, Small InterferingUbiquitin-Activating EnzymesATG7 protein, humanAutophagy-Related Protein 7CASP9 protein, humanCaspase 9MAP1LC3A protein, humanMicrotubule-Associated ProteinsMultienzyme ComplexesRNA, Small InterferingUbiquitin-Activating EnzymesApoptosisAutophagyCaspaseCell DeathCellular Regulation

Identifiers

PMID24362031
PMCPMC3945314
OpenAlexW2045457634

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.