Lysine acetylation and cancer: A proteomics perspective

Gil, Jeovanis; Ramírez-Torres, Alberto; Encarnación‐Guevara, Sergio

doi:10.1016/j.jprot.2016.10.003

Cited by 147 publications

(103 citation statements)

References 130 publications

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“…The abnormality of acetylation modifications is associated with diabetes, cardiovascular diseases, cancers, and neurodegenerative disorders [14–24]. During the last decade, proteomic studies have identified lysine acetylation in thousands of eukaryotic proteins which significantly expanded our knowledge of protein acetylation [25–27].…”

Section: Introductionmentioning

confidence: 99%

Studying the Lysine Acetylation of Malate Dehydrogenase

Venkat

Gregory

Sturges

et al. 2017

Journal of Molecular Biology

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Protein acetylation plays important roles in many biological processes. Malate dehydrogenase (MDH), a key enzyme in the tricarboxylic acid (TCA) cycle, has been identified to be acetylated in bacteria by proteomic studies, but no further characterization has been reported. One challenge for studying protein acetylation is to get purely acetylated proteins at specific positions. Here we applied the genetic code expansion strategy to site-specifically incorporate Nε-acetyllysine into MDH. The acetylation of lysine residues in MDH could enhance its enzyme activity. The Escherichia coli deacetylase CobB could deacetylate acetylated MDH, while the E. coli acetyltransferase YfiQ cannot acetylate MDH efficiently. Our results also demonstrated that acetyl-CoA or acetyl-phosphate could acetylate MDH chemically in vitro. Furthermore, the acetylation level of MDH was shown to be affected by carbon sources in the growth medium.

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Section: Introductionmentioning

confidence: 99%

Studying the Lysine Acetylation of Malate Dehydrogenase

Venkat

Gregory

Sturges

et al. 2017

Journal of Molecular Biology

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“…They catalyze the acetylation of histones to transcriptionally activate target genes. More importantly, CBP/p300‐modified nonhistone substrates also play critical roles in cancer progression . SGC‐CBP30, a compound that exhibits high selectivity for CBP/P300, markedly inhibits cell growth in several prostate cancer cell lines .…”

Section: Targeting Novel Dynamic Ptms In Cancer Therapymentioning

confidence: 99%

Advances of Proteomics in Novel PTM Discovery: Applications in Cancer Therapy

Wang

Zhang

et al. 2019

Small Methods

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Protein posttranslational modification (PTM) is a critical mechanism to enhance the diversity of protein species and functions in organisms. Currently, many different PTMs are discovered and found to be involved in a wide range of cellular processes. The aberrant regulation of PTM dynamics is reported to contribute to cancer development. Phosphorylation and acetylation are the best studied PTMs, and the application of high‐resolution mass spectrometry‐based proteomics and specific antibody‐based enrichment technologies significantly promotes novel PTM discovery. This review discusses methods for global PTM identification, including antibody‐based enrichment and chemical probe‐based identification. Several acylations, such as propionylation, butyrylation, succinylation, malonylation, and crotonylation, are recently found to influence both histone and nonhistone proteins and to be intimately linked with the progression of cancer. It is proposed that targeting novel PTM dynamics by pharmacological inhibitors has great potential for cancer therapy.

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“…Both bioinformatic analysis and experimental evidence suggest that there are likely other acetyltransferases existing in the cell with sequence,s tructure,a nd function distinct from the currently known KATs. [126] More work is needed to clarify the different roles of enzymatic versus non-enzymatic lysine acylation in cell biology.W ee nvision increasing "omics" discoveries on cellular acyltransferase enzymes and acylated protein substrates will not only provide an enhanced understanding of lysine acetylation and acylation in biological regulation, but also new diagnostic and therapeutic opportunities to tackle acetylation-regulated diseases. [124] Recent data show that several KATs,a side from their acetyltransferase activity,h ave novel acyltransferase activity.…”

Section: Summary and Perspectivementioning

confidence: 99%

Chemical Biology Approaches for Investigating the Functions of Lysine Acetyltransferases

Han

Liu

et al. 2017

Angew Chem Int Ed

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The side-chain acetylation of lysine residues in histones and non-histone proteins catalyzed by lysine acetyltransferases (KATs) represents a widespread posttranslational modification (PTM) in the eukaryotic cells. Lysine acetylation plays regulatory roles in major cellular pathways inside and outside the nucleus. In particular, KAT-mediated histone acetylation has an effect on all DNA-templated epigenetic processes. Aberrant expression and activation of KATs are commonly observed in human diseases, especially cancer. In recent years, the study of KAT functions in biology and disease has greatly benefited from chemical biology tools and strategies. In this Review, we present the past and current accomplishments in the design of chemical biology approaches for the interrogation of KAT activity and function. These methods and probes are classified according to their mechanisms of action and respective applications, with both strengths and limitations discussed.

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Lysine acetylation and cancer: A proteomics perspective

Cited by 147 publications

References 130 publications

Studying the Lysine Acetylation of Malate Dehydrogenase

Studying the Lysine Acetylation of Malate Dehydrogenase

Advances of Proteomics in Novel PTM Discovery: Applications in Cancer Therapy

Chemical Biology Approaches for Investigating the Functions of Lysine Acetyltransferases

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