Evidence map›Paper›PMID 31204282›Full record

ArticleCell metabolism2019

Transient Receptor Potential V Channels Are Essential for Glucose Sensing by Aldolase and AMPK.

Mengqi Li, Chen-Song Zhang, Yue Zong, Jin-Wei Feng, Teng Ma, Meiqin Hu, Zhizhong Lin, Xiaotong Li, Changchuan Xie, Yaying Wu and 21 more

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in Cell metabolism, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
15.2field-weighted citation impact, top 1% 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

95 citing papers in PubMed, 139 citations in OpenAlex.

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  16. Bioenergetics and metabolism of the pulmonary endothelium. Scientific session I: ReSPIRE 2025.American journal of physiology. Lung cellular and molecular physiology · 2025
    Review
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35 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

31 authors at 8 institutions in 3 countries.

Mengqi LiState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Chen-Song ZhangState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Yue ZongState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Jin-Wei FengState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Teng MaState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Meiqin HuState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, PKU-IDG/McGovern Institute for Brain Research, Peking University, 100871 Beijing, China.
Zhizhong LinState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Xiaotong LiState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Changchuan XieState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Yaying WuState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Dong JiangState Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.
Ying LiState Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.
Cixiong ZhangState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Xiao TianState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Wen WangCAS Key Laboratory of Separation Science for Analytical Chemistry, Scientific Research Center for Translational Medicine, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 116023 Dalian, China.
Yanyan YangState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Peking-Tsinghua Center for Life Sciences, Peking University, 100871 Beijing, China.
Jie ChenState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Peking-Tsinghua Center for Life Sciences, Peking University, 100871 Beijing, China.
Jiwen CuiState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Yu-Qing WuState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Xin ChenState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Qing-Feng LiuState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Jianfeng WuState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Shu-Yong LinState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Zhiyun YeState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China.
Ying LiuState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, Peking-Tsinghua Center for Life Sciences, Peking University, 100871 Beijing, China.
Hai-Long PiaoCAS Key Laboratory of Separation Science for Analytical Chemistry, Scientific Research Center for Translational Medicine, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, 116023 Dalian, China.
Li YuState Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.
Zhuan ZhouState Key Laboratory of Membrane Biology, Institute of Molecular Medicine, PKU-IDG/McGovern Institute for Brain Research, Peking University, 100871 Beijing, China.
Xiao-Song XieMcDermott Center of Human Growth and Development MC8591, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
D Grahame HardieDivision of Cell Signalling and Immunology, College of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland.
Sheng-Cai LinState Key Laboratory for Cellular Stress Biology, Innovation Center for Cell Signaling Network, School of Life Sciences, Xiamen University, 361102 Fujian, China. Electronic address: linsc@xmu.edu.cn.
Xiamen University · CNPeking University · CNTsinghua University · CNCenter for Life Sciences · CNChinese Academy of Sciences · CNDalian Institute of Chemical Physics · CNThe University of Texas Southwestern Medical Center · USUniversity of Dundee · GB

Funding

Wellcome Trust 204766/Z/16/Z
6 · The paper itself

Abstract

Fructose-1,6-bisphosphate (FBP) aldolase links sensing of declining glucose availability to AMPK activation via the lysosomal pathway. However, how aldolase transmits lack of occupancy by FBP to AMPK activation remains unclear. Here, we show that FBP-unoccupied aldolase interacts with and inhibits endoplasmic reticulum (ER)-localized transient receptor potential channel subfamily V, inhibiting calcium release in low glucose. The decrease of calcium at contact sites between ER and lysosome renders the inhibited TRPV accessible to bind the lysosomal v-ATPase that then recruits AXIN:LKB1 to activate AMPK independently of AMP. Genetic depletion of TRPVs blocks glucose starvation-induced AMPK activation in cells and liver of mice, and in nematodes, indicative of physical requirement of TRPVs. Pharmacological inhibition of TRPVs activates AMPK and elevates NAD

Indexed as

AcrylamidesAdenosine TriphosphatasesAMP-Activated Protein KinasesAnimalsBridged Bicyclo Compounds, HeterocyclicCaenorhabditis elegansCalciumCalcium ChannelsEndoplasmic ReticulumEnzyme ActivationFructose-Bisphosphate AldolaseGene Knockout TechniquesGlucoseHEK293 CellsHumansLysosomes3-(4-t-butylphenyl)-N-(2,3-dihydrobenzo(b)(1,4)dioxin-6-yl)acrylamideAcrylamidesAdenosine TriphosphatasesAMP-Activated Protein KinasesBridged Bicyclo Compounds, HeterocyclicCalciumCalcium ChannelsFructose-Bisphosphate AldolaseGlucoseTRPV Cation ChannelsaldolaseAMP-activated protein kinaseAMPKglucose sensingtransient receptor potential channelsTRPVv-ATPase

Identifiers

PMID31204282
PMCPMC6720459
OpenAlexW2949336437

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.