Destabilization of Fatty Acid Synthase by Acetylation Inhibits De Novo Lipogenesis and Tumor Cell Growth

Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacologic inhibitors of FASN are being evaluated in clinical trials for treatment of cancer, obesity, and other diseases. Here, we report a previously unknown mechanism of FASN re...

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Published inCancer research (Chicago, Ill.) Vol. 76; no. 23; pp. 6924 - 6936
Main Authors Lin, Huai-Peng, Cheng, Zhou-Li, He, Ruo-Yu, Song, Lei, Tian, Meng-Xin, Zhou, Li-Sha, Groh, Beezly S., Liu, Wei-Ren, Ji, Min-Biao, Ding, Chen, Shi, Ying-Hong, Guan, Kun-Liang, Ye, Dan, Xiong, Yue
Format Journal Article
LanguageEnglish
Published United States 01.12.2016
Subjects
Acetylation
Cell Growth Processes - genetics
Cell Proliferation
Fatty Acid Synthases - genetics
Humans
Lipogenesis - genetics
Signal Transduction
Tumor Microenvironment
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Abstract Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacologic inhibitors of FASN are being evaluated in clinical trials for treatment of cancer, obesity, and other diseases. Here, we report a previously unknown mechanism of FASN regulation involving its acetylation by KAT8 and its deacetylation by HDAC3. FASN acetylation promoted its degradation via the ubiquitin–proteasome pathway. FASN acetylation enhanced its association with the E3 ubiquitin ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. Our results suggest opportunities to target FASN acetylation as an anticancer strategy. Cancer Res; 76(23); 6924–36. ©2016 AACR.
AbstractList Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacologic inhibitors of FASN are being evaluated in clinical trials for treatment of cancer, obesity, and other diseases. Here, we report a previously unknown mechanism of FASN regulation involving its acetylation by KAT8 and its deacetylation by HDAC3. FASN acetylation promoted its degradation via the ubiquitin-proteasome pathway. FASN acetylation enhanced its association with the E3 ubiquitin ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. Our results suggest opportunities to target FASN acetylation as an anticancer strategy. Cancer Res; 76(23); 6924-36. ©2016 AACR.Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacologic inhibitors of FASN are being evaluated in clinical trials for treatment of cancer, obesity, and other diseases. Here, we report a previously unknown mechanism of FASN regulation involving its acetylation by KAT8 and its deacetylation by HDAC3. FASN acetylation promoted its degradation via the ubiquitin-proteasome pathway. FASN acetylation enhanced its association with the E3 ubiquitin ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. Our results suggest opportunities to target FASN acetylation as an anticancer strategy. Cancer Res; 76(23); 6924-36. ©2016 AACR.
Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacological inhibitors of FASN are being evaluated in clinical trials for treatment of cancer, obesity and other diseases. Here we report a previously unknown mechanism of FASN regulation involving its acetylation by KAT8 and its deacetylation by HDAC3. FASN acetylation promoted its degradation via the ubiquitin-proteasome pathway. FASN acetylation enhanced its association with the E3 ubiquitin-ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. Our results suggest opportunities to target FASN acetylation as an anticancer strategy.
Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacologic inhibitors of FASN are being evaluated in clinical trials for treatment of cancer, obesity, and other diseases. Here, we report a previously unknown mechanism of FASN regulation involving its acetylation by KAT8 and its deacetylation by HDAC3. FASN acetylation promoted its degradation via the ubiquitin-proteasome pathway. FASN acetylation enhanced its association with the E3 ubiquitin ligase TRIM21. Acetylation destabilized FASN and resulted in decreased de novo lipogenesis and tumor cell growth. FASN acetylation was frequently reduced in human hepatocellular carcinoma samples, which correlated with increased HDAC3 expression and FASN protein levels. Our results suggest opportunities to target FASN acetylation as an anticancer strategy. Cancer Res; 76(23); 6924-36. ©2016 AACR.
Author Zhou, Li-Sha
Groh, Beezly S.
Xiong, Yue
Liu, Wei-Ren
Ding, Chen
Ye, Dan
Ji, Min-Biao
Shi, Ying-Hong
Lin, Huai-Peng
Cheng, Zhou-Li
Song, Lei
Guan, Kun-Liang
He, Ruo-Yu
Tian, Meng-Xin
AuthorAffiliation 4 Department of Liver Surgery, Liver Cancer Institute, Zhongshan Hospital, Fudan University; Key Laboratory of Carcinogenesis and Cancer Invasion of Ministry of Education, Shanghai, 200032, China
7 Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, North Carolina 27599
3 State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, National Center for National Center for Protein Science (The PHOENIX Center), Beijing 102206, China
6 Department of General Surgery, Huashan Hospital, Fudan University, Shanghai 200040, China
2 State Key Laboratory of Surface Physics and Department of Physics, Fudan University, Shanghai, 200433, China
5 Department of Pharmacology and Moores Cancer Center, University of California San Diego, La Jolla, California 92093
1 Molecular and Cell Biology Lab, Institute of Biomedical Sciences, Shanghai Medical College; Key Laboratory of Metabolism an
AuthorAffiliation_xml – name: 2 State Key Laboratory of Surface Physics and Department of Physics, Fudan University, Shanghai, 200433, China
– name: 1 Molecular and Cell Biology Lab, Institute of Biomedical Sciences, Shanghai Medical College; Key Laboratory of Metabolism and Molecular Medicine, Ministry of Education, and Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences; State Key Laboratory of Genetic Engineering, Collaborative Innovation Center of Genetics and Development, School of Life Sciences, Fudan University, Shanghai 200032, China
– name: 3 State Key Laboratory of Proteomics, Beijing Proteome Research Center, Beijing Institute of Radiation Medicine, National Center for National Center for Protein Science (The PHOENIX Center), Beijing 102206, China
– name: 4 Department of Liver Surgery, Liver Cancer Institute, Zhongshan Hospital, Fudan University; Key Laboratory of Carcinogenesis and Cancer Invasion of Ministry of Education, Shanghai, 200032, China
– name: 6 Department of General Surgery, Huashan Hospital, Fudan University, Shanghai 200040, China
– name: 7 Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, North Carolina 27599
– name: 5 Department of Pharmacology and Moores Cancer Center, University of California San Diego, La Jolla, California 92093
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Snippet Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacologic inhibitors of FASN are being...
Fatty acid synthase (FASN) is the terminal enzyme in de novo lipogenesis and plays a key role in cell proliferation. Pharmacological inhibitors of FASN are...
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pubmed
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SourceType Open Access Repository
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StartPage 6924
SubjectTerms Acetylation
Cell Growth Processes - genetics
Cell Proliferation
Fatty Acid Synthases - genetics
Humans
Lipogenesis - genetics
Signal Transduction
Tumor Microenvironment
Title Destabilization of Fatty Acid Synthase by Acetylation Inhibits De Novo Lipogenesis and Tumor Cell Growth
URI https://www.ncbi.nlm.nih.gov/pubmed/27758890
https://www.proquest.com/docview/1835493240
https://pubmed.ncbi.nlm.nih.gov/PMC5135623
Volume 76
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