Evidence map›Paper›PMID 27626315›Full record

ArticleOncotarget2016

Fyn phosphorylates AMPK to inhibit AMPK activity and AMP-dependent activation of autophagy.

Eijiro Yamada, Shuichi Okada, Claire C Bastie, Manu Vatish, Yasuyo Nakajima, Ryo Shibusawa, Atsushi Ozawa, Jeffrey E Pessin, Masanobu Yamada

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.1field-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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Autophagy as a Guardian of Vascular Niche Homeostasis.International journal of molecular sciences · 2024
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  14. Honokiol Protects against Anti-Oxidative medicine and cellular longevity · 2018
    Article
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  16. Review
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

9 authors at 4 institutions in 3 countries.

Eijiro YamadaDepartment of Medicine and Molecular Science, Gunma University Graduate School of Medicine, Maebashi, Japan.
Shuichi OkadaDepartment of Medicine and Molecular Science, Gunma University Graduate School of Medicine, Maebashi, Japan.
Claire C BastieDivision of Biomedical Sciences, Warwick Medical School, Coventry, West Midlands, United Kingdom.
Manu VatishNuffield Department of Obstetrics & Gynaecology, University of Oxford, Oxford, United Kingdom.
Yasuyo NakajimaDepartment of Medicine and Molecular Science, Gunma University Graduate School of Medicine, Maebashi, Japan.
Ryo ShibusawaDepartment of Medicine and Molecular Science, Gunma University Graduate School of Medicine, Maebashi, Japan.
Atsushi OzawaDepartment of Medicine and Molecular Science, Gunma University Graduate School of Medicine, Maebashi, Japan.
Jeffrey E PessinDepartments of Medicine and Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York, United States of America.
Masanobu YamadaDepartment of Medicine and Molecular Science, Gunma University Graduate School of Medicine, Maebashi, Japan.
Gunma University · JPAlbert Einstein College of Medicine · USUniversity of Oxford · GBUniversity of Warwick · GB

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
RESEARCH TRAININGP30DK026687 · NIDDK · ST. LUKE'S-ROOSEVELT INST FOR HLTH SCIS · PI Anthony W Ferrante, DYMPNA GALLAGHER · 1986 to 2026
$33.0M
REGULATION OF THE INSULIN RECEPTOR KINASER01DK033823 · NIDDK · UNIVERSITY OF IOWA · PI KURLAND, IRWIN JACK, PESSIN, JEFFREY E. · 1986 to 2022
$6.7M
NCI NIH HHS P30 CA013330NIDDK NIH HHS P30 DK026687NIDDK NIH HHS R01 DK033823
6 · The paper itself

Abstract

We previously demonstrated that proto-oncogene Fyn decreased energy expenditure and increased metabolic phenotypes. Also Fyn decreased autophagy-mediated muscle mass by directly inhibiting LKB1 and stimulating STAT3 activities, respectively. AMPK, a downstream target of LKB1, was recently identified as a key molecule controlling autophagy. Here we identified that Fyn phosphorylates the α subunit of AMPK on Y436 and inhibits AMPK enzymatic activity without altering the assembly state of the AMPK heterotrimeric complex. As pro-inflammatory mediators are reported modulators of the autophagy processes, treatment with the pro-inflammatory cytokine TNFα resulted in 1) increased Fyn activity 2) stimulated Fyn-dependent AMPKα tyrosine phosphorylation and 3) decreased AICAR-dependent AMPK activation. Importantly, TNFα induced inhibition of autophagy was not observed when AMPKα was mutated on Y436. 4) These data demonstrate that Fyn plays an important role in relaying the effects of TNFα on autophagy and apoptosis via phosphorylation and inhibition of AMPK.

Indexed as

AutophagyAdenosine MonophosphateAMP-Activated Protein KinasesAnimalsApoptosisCell LineEnzyme ActivationHumansMiceMuscle, SkeletalPhosphorylationProto-Oncogene MasProto-Oncogene Proteins c-fynStress, PhysiologicalTumor Necrosis Factor-alphaAdenosine MonophosphateAMP-Activated Protein KinasesMAS1 protein, humanProto-Oncogene MasProto-Oncogene Proteins c-fynTumor Necrosis Factor-alphaAMPKAutophagyFynTNFα

Identifiers

PMID27626315
PMCPMC5340180
OpenAlexW2507121647

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.