Evidence map›Paper›PMID 30425250›Full record

ArticleNature communications2018

Proteome-wide analysis of USP14 substrates revealed its role in hepatosteatosis via stabilization of FASN.

Bin Liu, Shangwen Jiang, Min Li, Xuelian Xiong, Mingrui Zhu, Duanzhuo Li, Lei Zhao, Lili Qian, Linhui Zhai, Jing Li and 6 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed, 1 pooled it
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

90 citing papers in PubMed, 1 synthesis or guideline pooled it, 184 citations in OpenAlex.

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30 more citing papers are in PubMed but not listed here.

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

16 authors at 6 institutions in 2 countries.

Bin LiuDepartment of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University, Shanghai, 200032, PR China.
Shangwen JiangState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Min LiDepartment of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University, Shanghai, 200032, PR China.
Xuelian XiongDepartment of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University, Shanghai, 200032, PR China.
Mingrui ZhuState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Duanzhuo LiHubei Key Laboratory for Kidney Disease Pathogenesis and Intervention, Hubei Polytechnic University School of Medicine, Huangshi, Hubei, 435003, PR China.
Lei ZhaoState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Lili QianState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Linhui ZhaiState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Jing LiDepartment of Bioinformatics and Biostatistics, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, PR China.ORCID http://orcid.org/0000-0003-4602-3227
Han LuDepartment of Anesthesiology, Ruijin Hospital, Shanghai Jiao-Tong University School of Medicine (SJTU-SM), Shanghai, 200025, PR China.
Shengnan SunState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China.
Jiandie LinLife Sciences Institute and Department of Cell and Developmental Biology, University of Michigan Medical Center, Ann Arbor, MI, USA.
Yan LuDepartment of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University, Shanghai, 200032, PR China. lu.yan2@zs-hospital.sh.cn.ORCID http://orcid.org/0000-0001-8069-5647
Xiaoying LiDepartment of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University, Shanghai, 200032, PR China. li.xiaoying@zs-hospital.sh.cn.
Minjia TanState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, 201203, PR China. mjtan@simm.ac.cn.ORCID http://orcid.org/0000-0002-6784-9653
Chinese Academy of Sciences · CNFudan University · CNShanghai Jiao Tong University · CNHubei Polytechnic University · CNShanghai Institute of Materia Medica · CNUniversity of Michigan · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitin-specific protease 14 (USP14) is one of the major proteasome-associated deubiquitinating enzymes critical for proteome homeostasis. However, substrates of USP14 remain largely unknown, hindering the understanding of its functional roles. Here we conduct a comprehensive proteome, ubiquitinome and interactome analysis for USP14 substrate screening. Bioinformatics analysis reveals broad new potential roles of USP14, especially in lipid and carbohydrate metabolism. Among the potential substrates identified, we show that fatty acid synthase (FASN), a key enzyme involved in hepatic lipogenesis, is a bona fide substrate of USP14. USP14 directly interacts with and increases FASN stability. As a result, overexpression of USP14 promotes liver triglyceride accumulation in C57BL/6 mice, whereas genetic ablation or pharmacological inhibition of USP14 ameliorates hepatosteatosis, hyperglycemia and insulin resistance in obese mice. In conclusion, our findings reveal for the first time an indispensable role of USP14 in hepatosteatosis through FASN stabilization.

Indexed as

ProteomeAnimalsCarbohydrate MetabolismComputational BiologyFatty Acid SynthasesGene Knockdown TechniquesHomeostasisHumansHyperglycemiaInsulin ResistanceLipogenesisLiverMaleMiceMice, Inbred C57BLMice, ObeseFatty Acid SynthasesProteomeTriglyceridesUbiquitin ThiolesteraseUsp14 protein, mouse

Identifiers

PMID30425250
PMCPMC6233205
OpenAlexW2899910765

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.