Evidence map›Paper›PMID 32809272›Full record

ArticleCancer communications (London, England)2020

A newly discovered role of metabolic enzyme PCK1 as a protein kinase to promote cancer lipogenesis.

Hongfei Jiang, Lei Zhu, Daqian Xu, Zhimin Lu

Open access · goldAbstract readEditorial
In one paragraph

Article in Cancer communications (London, England), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.9field-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

28 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  3. Inhibition of Tumor Lipogenesis and Growth by Peptide-Based Targeting of SREBP Activation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
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  19. Liver fat metabolism of broilers regulated byFrontiers in microbiology · 2022
    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

4 authors at 2 institutions in 1 country.

Hongfei JiangThe Affiliated Hospital of Qingdao University and Qingdao Cancer Institute, Qingdao, Shandong, 266071, P. R. China.
Lei ZhuThe Affiliated Hospital of Qingdao University and Qingdao Cancer Institute, Qingdao, Shandong, 266071, P. R. China.
Daqian XuDepartment of Hepatobiliary and Pancreatic Surgery, Zhejiang Provincial Key Laboratory of Pancreatic Disease, Institute of Translational Medicine, the First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310029, P. R. China.
Zhimin LuDepartment of Hepatobiliary and Pancreatic Surgery, Zhejiang Provincial Key Laboratory of Pancreatic Disease, Institute of Translational Medicine, the First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, Zhejiang, 310029, P. R. China.ORCID 0000-0002-2859-2736
Qingdao University · CNZhejiang University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Highly active lipogenesis is essential for rapid tumor growth. Sterol regulatory element-binding protein (SREBP) is a key transcriptional factor for lipogenesis and activated by reduced sterol and oxysterol levels. However, the mechanism by which cancer cells activate SREBP without altering these sterol/oxysterol levels remains elusive. In one of our recent studies published in Nature entitled "The gluconeogenic enzyme PCK1 phosphorylates INSIG1/2 for lipogenesis", we demonstrated that activated AKT-mediated phosphoenolpyruvate carboxykinase 1 (PCK1) S90 phosphorylation reduces the gluconeogenic activity of PCK1 and triggers its translocation to the endoplasmic reticulum (ER), where PCK1 acts as a protein kinase and uses GTP, rather than ATP, as a phosphate donor to phosphorylate Insig1/2 thereby reducing oxysterol's binding to Insig1/2 and activating SREBP-mediated lipogenesis for tumor growth. These findings elucidate a coordinated regulation between gluconeogenesis and lipogenesis and uncover a critical role of the protein kinase activity of PCK1 in SREBP-dependent lipid synthesis.

Indexed as

LipogenesisNeoplasmsHumansIntracellular Signaling Peptides and ProteinsPhosphoenolpyruvate Carboxykinase (GTP)PhosphorylationProtein KinasesSterol Regulatory Element Binding Protein 1Intracellular Signaling Peptides and ProteinsPCK1 protein, humanPhosphoenolpyruvate Carboxykinase (GTP)Protein KinasesSREBF1 protein, humanSterol Regulatory Element Binding Protein 1

Identifiers

PMID32809272
PMCPMC7494067
OpenAlexW3080734379

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.