Global profiling of crotonylation on non-histone proteins

Xu, Weizhi; Wan, Junhu; Zhan, Jun; Li, Xueying; He, Huiying; Shi, Zhaomei; Zhang, Hongquan

doi:10.1038/cr.2017.60

Cited by 151 publications

(188 citation statements)

References 9 publications

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“…In recent years, several landmark studies have revealed dramatically improved number of crotonylated lysine residues and crotonylated proteins (Table 1), and these proteins play roles in nearly all cellular processes including chromatin remodelling, metabolism, cell cycle and cellular organization. [13][14][15][16][17][18][19][20][21][22] Crotonylome mapping provides an important resource for discovering novel properties and regulatory functions of crotonylation.…”

Section: Protein Crotonylomementioning

confidence: 99%

Functions and mechanisms of lysine crotonylation

Wan

Chu

et al. 2019

J Cellular Molecular Medi

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Lysine crotonylation is a newly discovered post‐translational modification, which is structurally and functionally different from the widely studied lysine acetylation. Recent advances in the identification and quantification of lysine crotonylation by mass spectrometry have revealed that non‐histone proteins are frequently crotonylated, implicating it in many biological processes through the regulation of chromatin remodelling, metabolism, cell cycle and cellular organization. In this review, we summarize the writers, erasers and readers of lysine crotonylation, and their physiological functions, including gene transcription, acute kidney injury, spermatogenesis, depression, telomere maintenance, HIV latency and cancer process. These findings not only point to the new functions for lysine crotonylation, but also highlight the mechanisms by which crotonylation regulates various cellular processes.

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Section: Protein Crotonylomementioning

confidence: 99%

Functions and mechanisms of lysine crotonylation

Wan

Chu

et al. 2019

J Cellular Molecular Medi

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“…In order to confirm dynamic acetylation and crotonylation modifications in obesity, we performed immunoblotting and coimmunoprecipitation with pan anti-Kar and pan anti-Kcr antibodies. 2,7,11,12 Taken together, we show the dynamic interactions of acetylation and crotonylation modification of non-histone proteins in obesity and anti-obesity. And the expression level of Dld protein increased slightly in anti-obesity process ( Figure 2C).…”

mentioning

confidence: 61%

“…Therefore, we proposed the hypothesis that the equilibrium between acetylation and crotonylation of non-histone protein was determined by the relative concentrations of crotonyl-CoA and acetyl-CoA in cells, which was consistent with previous studies. 2,7,11,12 Taken together, we show the dynamic interactions of acetylation and crotonylation modification of non-histone proteins in obesity and anti-obesity. These non-histone proteins are involved in multiple signalling pathways and regulate cellular functions, particularly in TCA cycle.…”

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confidence: 61%

“…2,3 Acetylases and deacetylases are identified to function in both lysine acetylation and lysine crotonylation. Lysine crotonylation occurs primarily on the ε-amino group of lysine, but its planar orientation and four carbon length distinguish it from lysine acetylation.…”

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confidence: 99%

“…Lysine crotonylation occurs primarily on the ε-amino group of lysine, but its planar orientation and four carbon length distinguish it from lysine acetylation. 2,3 Acetylases and deacetylases are identified to function in both lysine acetylation and lysine crotonylation. [4][5][6] Lysine crotonylation is a more potent transcriptional activator than lysine acetylation.…”

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confidence: 99%

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Dynamic post‐translational modifications in obesity

Yang

et al. 2019

J Cellular Molecular Medi

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Post-translational modifications (PTMs) of histone and non-histone proteins orchestrate metabolic reprogramming and immune responses in obesity. Particularly, PTMs of non-histone proteins are essential for signal transduction in metabolic reprogramming of adipose tissue, which are ectopic deposition in obesity. 1 BothThis is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

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Chemical Biology Tools for Protein Lysine Acylation

Xie

Liu

et al. 2022

Angewandte Chemie

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Lysine acylation plays pivotal roles in cell physiology, including DNA transcription and repair, signal transduction, immune defense, metabolism, and many other key cellular processes. Molecular mechanisms of dysregulated lysine acylation are closely involved in the pathophysiological progress of many human diseases, most notably cancers. In recent years, chemical biology tools have become instrumental in studying the function of post‐translational modifications (PTMs), identifying new “writers”, “erasers” and “readers”, and in targeted therapies. Here, we describe key developments in chemical biology approaches that have advanced the study of lysine acylation and its regulatory proteins (2016–2021). We further discuss the discovery of ligands (inhibitors and PROTACs) that are capable of targeting regulators of lysine acylation. Next, we discuss some current challenges of these chemical biology probes and suggest how chemists and biologists can utilize chemical probes with more discriminating capacity. Finally, we suggest some critical considerations in future studies of PTMs from our perspective.

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Global profiling of crotonylation on non-histone proteins

Cited by 151 publications

References 9 publications

Functions and mechanisms of lysine crotonylation

Functions and mechanisms of lysine crotonylation

Dynamic post‐translational modifications in obesity

Chemical Biology Tools for Protein Lysine Acylation

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