Literature DB >> 34061242

Protein acetylation: a novel modus of obesity regulation.

Yuexia Liu1, Hong Yang1, Xuanchen Liu1, Huihui Gu1, Yizhou Li1, Chao Sun2.   

Abstract

Obesity is a chronic epidemic disease worldwide which has become one of the important public health issues. It is a process that excessive accumulation of adipose tissue caused by long-term energy intake exceeding energy expenditure. So far, the prevention and treatment strategies of obesity on individuals and population have not been successful in the long term. Acetylation is one of the most common ways of protein post-translational modification (PTM). It exists on thousands of non-histone proteins in almost every cell chamber. It has many influences on protein levels and metabolome levels, which is involved in a variety of metabolic reactions, including sugar metabolism, tricarboxylic acid cycle, and fatty acid metabolism, which are closely related to biological activities. Studies have shown that protein acetylation levels are dynamically regulated by lysine acetyltransferases (KATs) and lysine deacetylases (KDACs). Protein acetylation modifies protein-protein and protein-DNA interactions and regulates the activity of enzymes or cytokines which is related to obesity in order to participate in the occurrence and treatment of obesity-related metabolic diseases. Therefore, we speculated that acetylation was likely to become effective means of controlling obesity in the future. In consequence, this review focuses on the mechanisms of protein acetylation controlled obesity, to provide theoretical basis for controlling obesity and curing obesity-related diseases, which is a significance for regulating obesity in the future. This review will focus on the role of protein acetylation in controlling obesity.
© 2021. The Author(s), under exclusive licence to Springer-Verlag GmbH Germany, part of Springer Nature.

Entities:  

Keywords:  KATs; KDACs; Obesity; PTMs; Protein acetylation modification

Mesh:

Substances:

Year:  2021        PMID: 34061242     DOI: 10.1007/s00109-021-02082-2

Source DB:  PubMed          Journal:  J Mol Med (Berl)        ISSN: 0946-2716            Impact factor:   4.599


  115 in total

Review 1.  Protein acetylation in metabolism - metabolites and cofactors.

Authors:  Keir J Menzies; Hongbo Zhang; Elena Katsyuba; Johan Auwerx
Journal:  Nat Rev Endocrinol       Date:  2015-10-27       Impact factor: 43.330

Review 2.  Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.

Authors:  Ibraheem Ali; Ryan J Conrad; Eric Verdin; Melanie Ott
Journal:  Chem Rev       Date:  2018-02-06       Impact factor: 60.622

Review 3.  50 years of protein acetylation: from gene regulation to epigenetics, metabolism and beyond.

Authors:  Eric Verdin; Melanie Ott
Journal:  Nat Rev Mol Cell Biol       Date:  2014-12-30       Impact factor: 94.444

4.  Cell Wall Polymers: The Importance of Deacetylation.

Authors:  Nancy R Hofmann
Journal:  Plant Cell       Date:  2019-04-17       Impact factor: 11.277

Review 5.  Functions and mechanisms of non-histone protein acetylation.

Authors:  Takeo Narita; Brian T Weinert; Chunaram Choudhary
Journal:  Nat Rev Mol Cell Biol       Date:  2019-03       Impact factor: 94.444

Review 6.  Acetylation control of cardiac fatty acid β-oxidation and energy metabolism in obesity, diabetes, and heart failure.

Authors:  Arata Fukushima; Gary D Lopaschuk
Journal:  Biochim Biophys Acta       Date:  2016-07-29

7.  Rabbit N-acetyltransferase 2 genotyping method to investigate role of acetylation polymorphism on N- and O-acetylation of aromatic and heterocyclic amine carcinogens.

Authors:  David W Hein; Mark A Doll
Journal:  Arch Toxicol       Date:  2017-05-23       Impact factor: 5.153

8.  Evolution of a mass spectrometry-grade protease with PTM-directed specificity.

Authors:  Duc T Tran; Valerie J Cavett; Vuong Q Dang; Héctor L Torres; Brian M Paegel
Journal:  Proc Natl Acad Sci U S A       Date:  2016-12-08       Impact factor: 11.205

9.  Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis.

Authors:  Min-Xian Qian; Ye Pang; Cui Hua Liu; Kousuke Haratake; Bo-Yu Du; Dan-Yang Ji; Guang-Fei Wang; Qian-Qian Zhu; Wei Song; Yadong Yu; Xiao-Xu Zhang; Hai-Tao Huang; Shiying Miao; Lian-Bin Chen; Zi-Hui Zhang; Ya-Nan Liang; Shan Liu; Hwangho Cha; Dong Yang; Yonggong Zhai; Takuo Komatsu; Fuminori Tsuruta; Haitao Li; Cheng Cao; Wei Li; Guo-Hong Li; Yifan Cheng; Tomoki Chiba; Linfang Wang; Alfred L Goldberg; Yan Shen; Xiao-Bo Qiu
Journal:  Cell       Date:  2013-05-23       Impact factor: 41.582

10.  PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile.

Authors:  Yu Liu; Minghui Wang; Jianing Xi; Fenglin Luo; Ao Li
Journal:  Int J Biol Sci       Date:  2018-05-22       Impact factor: 6.580

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