Evidence map›Paper›PMID 29717115›Full record

ArticleNature communications2018

Non-canonical activation of DAPK2 by AMPK constitutes a new pathway linking metabolic stress to autophagy.

Ruth Shiloh, Yuval Gilad, Yaara Ber, Miriam Eisenstein, Dina Aweida, Shani Bialik, Shenhav Cohen, Adi Kimchi

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed, 2 pooled it
4.7field-weighted citation impact, top 4% 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

29 citing papers in PubMed, 2 syntheses or guidelines pooled it, 40 citations in OpenAlex.

  1. Pooled it
  2. Guideline
  3. Review
  4. Article
  5. The Biological Role and Clinical Significance of BECLIN-1 in Cancer.International journal of molecular sciences · 2025
    Review
  6. 1-L Transcription in Prion Diseases.International journal of molecular sciences · 2024
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Autophagy in metabolic disease and ageing.Nature reviews. Endocrinology · 2021
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Autophagy as a Potential Therapy for Malignant Glioma.Pharmaceuticals (Basel, Switzerland) · 2020
    Review
  20. Article
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

8 authors at 2 institutions in 1 country.

Ruth ShilohDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel.
Yuval GiladDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel.
Yaara BerDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel.
Miriam EisensteinDepartment of Chemical Research Support, Weizmann Institute of Science, Rehovot, 76100, Israel.
Dina AweidaFaculty of Biology, Technion Israel Institute of Technology, Haifa, 32000, Israel.
Shani BialikDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel.
Shenhav CohenFaculty of Biology, Technion Israel Institute of Technology, Haifa, 32000, Israel.
Adi KimchiDepartment of Molecular Genetics, Weizmann Institute of Science, Rehovot, 76100, Israel. adi.kimchi@weizmann.ac.il.
Weizmann Institute of Science · ILTechnion – Israel Institute of Technology · IL

Funding

ULTRASTRUCTURE AND CYTOMORPHOLOGY COREP30DK042086 · NIDDK · UNIVERSITY OF CHICAGO · PI LIU, CAMBRIAN YANGSHAO · 1990 to 2025
$29.8M
6 · The paper itself

Abstract

Autophagy is an intracellular degradation process essential for adaptation to metabolic stress. DAPK2 is a calmodulin-regulated protein kinase, which has been implicated in autophagy regulation, though the mechanism is unclear. Here, we show that the central metabolic sensor, AMPK, phosphorylates DAPK2 at a critical site in the protein structure, between the catalytic and the calmodulin-binding domains. This phosphorylation activates DAPK2 by functionally mimicking calmodulin binding and mitigating an inhibitory autophosphorylation, providing a novel, alternative mechanism for DAPK2 activation during metabolic stress. In addition, we show that DAPK2 phosphorylates the core autophagic machinery protein, Beclin-1, leading to dissociation of its inhibitor, Bcl-X

Indexed as

AutophagyStress, PhysiologicalA549 CellsAdenylate KinaseAmino Acid SequenceAnimalsbcl-X ProteinBeclin-1CatalysisDeath-Associated Protein KinasesDimerizationHCT116 CellsHEK293 CellsHumansMaleMiceAdenylate Kinasebcl-X ProteinBeclin-1BECN1 protein, humanDAPK2 protein, humanDeath-Associated Protein KinasesSerineThreonine

Identifiers

PMID29717115
PMCPMC5931534
OpenAlexW2807539574

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.