ArticleCell death & disease2018
p53 cooperates with SIRT6 to regulate cardiolipin de novo biosynthesis.
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Article in Cell death & disease, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21citing papers in PubMed
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21 citing papers in PubMed, 43 citations in OpenAlex.
- Emerging roles of SIRT6 and its modulators in kidney diseases.Cell death discovery · 2026Review
- Competitive antagonism of KAT7 crotonylation against acetylation affects procentriole formation and colorectal tumorigenesis.Nature communications · 2025Article
- A Barth Syndrome Patient-DerivedInternational journal of molecular sciences · 2024Article
- SIRT3 regulates cardiolipin biosynthesis in pressure overload-induced cardiac remodeling by PPARγ-mediated mechanism.PloS one · 2024Article
- KAT8 acetylation-controlled lipolysis affects the invasive and migratory potential of colorectal cancer cells.Cell death & disease · 2023Article
- Sirt6 protects cardiomyocytes against doxorubicin-induced cardiotoxicity by inhibiting P53/Fas-dependent cell death and augmenting endogenous antioxidant defense mechanisms.Cell biology and toxicology · 2023Article
- SIRT6 in Aging, Metabolism, Inflammation and Cardiovascular Diseases.Aging and disease · 2022Review
- The complexity of p53-mediated metabolic regulation in tumor suppression.Seminars in cancer biology · 2022Review
- Inhibition of AKT induces p53/SIRT6/PARP1-dependent parthanatos to suppress tumor growth.Cell communication and signaling : CCS · 2022Article
- Sirtuins and Renal Oxidative Stress.Antioxidants (Basel, Switzerland) · 2021Review
- Integrative analysis of somatic mutations and differential expression profiles in glioblastoma based on aging acceleration.International journal of clinical and experimental pathology · 2021Article
- SIRT6 as a key event linking P53 and NRF2 counteracts APAP-induced hepatotoxicity through inhibiting oxidative stress and promoting hepatocyte proliferation.Acta pharmaceutica Sinica. B · 2021Article
- Age-related epigenetic drift deregulatesEpigenetics · 2020Article
- Review
- SIRT6 coordinates with CHD4 to promote chromatin relaxation and DNA repair.Nucleic acids research · 2020Article
- The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy.Frontiers in cell and developmental biology · 2020Review
- Sirt6 Deacetylase: A Potential Key Regulator in the Prevention of Obesity, Diabetes and Neurodegenerative Disease.Frontiers in pharmacology · 2020Article
- CDP-Diacylglycerol Synthases (CDS): Gateway to Phosphatidylinositol and Cardiolipin Synthesis.Frontiers in cell and developmental biology · 2020Review
- Mitohormesis and metabolic health: The interplay between ROS, cAMP and sirtuins.Free radical biology & medicine · 2019Review
- Updates on the epigenetic roles of sirtuins.Current opinion in chemical biology · 2019Review
Corrections and comments
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Authors and funding
18 authors at 2 institutions in 3 countries.
Meiting LiKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Tianyun HouKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Tian GaoKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Xiaopeng LuGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Carson cancer research center, Department of Biochemistry and Molecular Biology, School of Medicine, Shenzhen University, Shenzhen, 516080, China.
Qiaoyan YangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Qian ZhuGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Carson cancer research center, Department of Biochemistry and Molecular Biology, School of Medicine, Shenzhen University, Shenzhen, 516080, China.
Zhiming LiKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Chaohua LiuKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Guanqun MuKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Ge LiuGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Carson cancer research center, Department of Biochemistry and Molecular Biology, School of Medicine, Shenzhen University, Shenzhen, 516080, China.
Yantao BaoGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Carson cancer research center, Department of Biochemistry and Molecular Biology, School of Medicine, Shenzhen University, Shenzhen, 516080, China.
He WenGuangdong Key Laboratory for Genome Stability and Human Disease Prevention, Carson cancer research center, Department of Biochemistry and Molecular Biology, School of Medicine, Shenzhen University, Shenzhen, 516080, China.
Lina WangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Haiying WangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Ying ZhaoKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China.
Wei GuInstitute for Cancer Genetics, Department of Pathology and Cell Biology, Herbert Irving Comprehensive Cancer Center, College of Physicians & Surgeons, Columbia University, 1130 Nicholas Ave, New York, NY, 10032, USA.
Yang YangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China. yangsh@bjmu.edu.cn.
Wei-Guo ZhuKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Beijing Key Laboratory of Protein Posttranslational Modifications and Cell Function, Department of Biochemistry and Molecular Biology, School of Basic Medical Sciences, Peking University Health Science Center, 38 Xueyuan Road, Beijing, 100191, China. zhuweiguo@szu.edu.cn.ORCID 0000-0001-8385-6581
Peking University · CNShenzhen University · CN
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tumor suppressor p53 has critical roles in regulating lipid metabolism, but whether and how p53 regulates cardiolipin (CL) de novo biosynthesis is unknown. Here, we report that p53 physically interacts with histone deacetylase SIRT6 in vitro and in vivo, and this interaction increases following palmitic acid (PA) treatment. In response to PA, p53 and SIRT6 localize to chromatin in a p53-dependent manner. Chromatin p53 and SIRT6 bind the promoters of CDP-diacylglycerol synthase 1 and 2 (CDS1 and CDS2), two enzymes required to catalyze CL de novo biosynthesis. Here, SIRT6 serves as a co-activator of p53 and effectively recruits RNA polymerase II to the CDS1 and CDS2 promoters to enhance CL de novo biosynthesis. Our findings reveal a novel, cooperative model executed by p53 and SIRT6 to maintain lipid homeostasis.
Indexed as
Blotting, WesternCardiolipinsDiacylglycerol CholinephosphotransferaseHCT116 CellsHep G2 CellsHumansImmunoprecipitationPromoter Regions, GeneticProtein BindingReal-Time Polymerase Chain ReactionRNA InterferenceSirtuinsTumor Suppressor Protein p53CardiolipinsCDS1 protein, humanCDS2 protein, humanDiacylglycerol CholinephosphotransferaseSIRT6 protein, humanSirtuinsTP53 protein, humanTumor Suppressor Protein p53
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