Evidence map›Paper›PMID 24317201›Full record

ArticleCell death and differentiation2014

Phospholipase D-mediated autophagic regulation is a potential target for cancer therapy.

Y H Jang, K Y Choi, D S Min

Abstract read
In one paragraph

Article in Cell death and differentiation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  10. Review
  11. SCD1, autophagy and cancer: implications for therapy.Journal of experimental & clinical cancer research : CR · 2021
    Review
  12. Article
  13. Article
  14. Roles of Autophagy in Oxidative Stress.International journal of molecular sciences · 2020
    Review
  15. mTOR-Related Cell-Clearing Systems in Epileptic Seizures, an Update.International journal of molecular sciences · 2020
    Review
  16. Review
  17. Article
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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

3 authors at 2 institutions in 1 country.

Y H JangDepartment of Molecular Biology, College of Natural Science, Pusan National University, Busan 609-735, Korea.
K Y ChoiTranslational Research Center for Protein Function Control, Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul, South Korea.
D S Min1] Department of Molecular Biology, College of Natural Science, Pusan National University, Busan 609-735, Korea [2] Translational Research Center for Protein Function Control, Department of Biotechnology, College of Life Science and Biotechnology, Yonsei University, Seoul, South Korea.
Yonsei University · KRPusan National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagy is a catabolic process in which cell components are degraded to maintain cellular homeostasis by nutrient limitations. Defects of autophagy are involved in numerous diseases, including cancer. Here, we demonstrate a new role of phospholipase D (PLD) as a regulator of autophagy. PLD inhibition enhances autophagic flux via ATG1 (ULK1), ATG5 and ATG7, which are essential autophagy gene products critical for autophagosome formation. Moreover, PLD suppresses autophagy by differentially modulating phosphorylation of ULK1 mediated by mTOR and adenosine monophosphate-activated protein kinase (AMPK), and by suppressing the interaction of Beclin 1 with vacuolar-sorting protein 34 (Vps34), indicating that PLD coordinates major players of the autophagic pathway, AMPK-mTOR-ULK1 and Vps34/Beclin 1. Ultimately, PLD inhibition significantly sensitized in vitro and in vivo cancer regression via genetic and pharmacological inhibition of autophagy, providing rationale for a new therapeutic approach to enhancing the anticancer efficacy of PLD inhibition. Collectively, we show a novel role for PLD in the molecular machinery regulating autophagy.

Indexed as

AutophagyAMP-Activated Protein KinasesAnimalsApoptosis Regulatory ProteinsAutophagy-Related Protein-1 HomologAutophagy-Related Protein 5Autophagy-Related Protein 7Beclin-1Cell LineHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMiceMice, Inbred BALB CAMP-Activated Protein KinasesApoptosis Regulatory ProteinsAtg5 protein, mouseAtg7 protein, mouseAutophagy-Related Protein-1 HomologAutophagy-Related Protein 5Autophagy-Related Protein 7Beclin-1BECN1 protein, humanIntracellular Signaling Peptides and ProteinsMembrane ProteinsMicrotubule-Associated ProteinsMTOR protein, humanPhosphodiesterase InhibitorsPhospholipase Dphospholipase D1Protein Serine-Threonine KinasesTOR Serine-Threonine KinasesULK1 protein, human

Identifiers

PMID24317201
PMCPMC3950317
OpenAlexW1972686405

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.