Evidence map›Paper›PMID 37828054›Full record

ArticleNature communications2023

Palmitoylation-driven PHF2 ubiquitination remodels lipid metabolism through the SREBP1c axis in hepatocellular carcinoma.

Do-Won Jeong, Jong-Wan Park, Kyeong Seog Kim, Jiyoung Kim, June Huh, Jieun Seo, Ye Lee Kim, Joo-Youn Cho, Kwang-Woong Lee, Junji Fukuda and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
15.3field-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

60 citing papers in PubMed, 64 citations in OpenAlex.

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  11. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
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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

11 authors at 3 institutions in 3 countries.

Do-Won JeongDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.ORCID 0000-0001-6358-534X
Jong-Wan ParkDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.ORCID 0000-0003-4676-5191
Kyeong Seog KimDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.
Jiyoung KimDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.ORCID 0000-0002-5892-1369
June HuhDepartment of Chemical and Biological Engineering, Korea University, Seoul, 02841, Korea.ORCID 0000-0002-4610-4521
Jieun SeoDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.ORCID 0000-0003-1319-832X
Ye Lee KimDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.
Joo-Youn ChoDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea.ORCID 0000-0001-9270-8273
Kwang-Woong LeeDepartment of Surgery, Seoul National University College of Medicine, Seoul, 03080, Korea.
Junji FukudaFaculty of Engineering, Yokohama National University, Yokohama, 240-8501, Japan.ORCID 0000-0002-7194-8099
Yang-Sook ChunDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, 03080, Korea. chunys@snu.ac.kr.
Seoul National University · KRKorea University · KRYokohama National University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Palmitic acid (PA) is the most common fatty acid in humans and mediates palmitoylation through its conversion into palmitoyl coenzyme A. Although palmitoylation affects many proteins, its pathophysiological functions are only partially understood. Here we demonstrate that PA acts as a molecular checkpoint of lipid reprogramming in HepG2 and Hep3B cells. The zinc finger DHHC-type palmitoyltransferase 23 (ZDHHC23) mediates the palmitoylation of plant homeodomain finger protein 2 (PHF2), subsequently enhancing ubiquitin-dependent degradation of PHF2. This study also reveals that PHF2 functions as a tumor suppressor by acting as an E3 ubiquitin ligase of sterol regulatory element-binding protein 1c (SREBP1c), a master transcription factor of lipogenesis. PHF2 directly destabilizes SREBP1c and reduces SREBP1c-dependent lipogenesis. Notably, SREBP1c increases free fatty acids in hepatocellular carcinoma (HCC) cells, and the consequent PA induction triggers the PHF2/SREBP1c axis. Since PA seems central to activating this axis, we suggest that levels of dietary PA should be carefully monitored in patients with HCC.

Indexed as

Carcinoma, HepatocellularLiver NeoplasmsHomeodomain ProteinsHumansLipid MetabolismLipoylationSterol Regulatory Element Binding Protein 1UbiquitinationHomeodomain ProteinsPHF2 protein, humanSterol Regulatory Element Binding Protein 1

Identifiers

PMID37828054
PMCPMC10570296
OpenAlexW4387577586

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.