Nature Communications (Nov 2018)
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,
- Han Lu,
- Shengnan Sun,
- Jiandie Lin,
- Yan Lu,
- Xiaoying Li,
- Minjia Tan
Affiliations
- Bin Liu
- Department of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University
- Shangwen Jiang
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- Min Li
- Department of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University
- Xuelian Xiong
- Department of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University
- Mingrui Zhu
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- Duanzhuo Li
- Hubei Key Laboratory for Kidney Disease Pathogenesis and Intervention, Hubei Polytechnic University School of Medicine
- Lei Zhao
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- Lili Qian
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- Linhui Zhai
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- Jing Li
- Department of Bioinformatics and Biostatistics, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University
- Han Lu
- Department of Anesthesiology, Ruijin Hospital, Shanghai Jiao-Tong University School of Medicine (SJTU-SM)
- Shengnan Sun
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- Jiandie Lin
- Life Sciences Institute and Department of Cell and Developmental Biology, University of Michigan Medical Center
- Yan Lu
- Department of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University
- Xiaoying Li
- Department of Endocrinology and Metabolism, Zhongshan Hospital, Fudan Institute of Metabolic Diseases, Key Laboratory of Metabolism and Molecular Medicine, the Ministry of Education, Fudan University
- Minjia Tan
- State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences
- DOI
- https://doi.org/10.1038/s41467-018-07185-y
- Journal volume & issue
-
Vol. 9,
no. 1
pp. 1 – 12
Abstract
Ubiquitin-specific protease 14 (USP14) is a proteasome-associated deubiquitinating enzyme with known roles in physiology and disease. Here the authors show that fatty acid synthase (FASN) is a substrate of USP14, and that by stabilizing FASN, it plays a role in hepatosteatosis.
