Details

Autor(en) / Beteiligte

• Xie, Yusheng
• Du, Shubo
• Liu, Zhiyang
• Liu, Min
• Xu, Zhiqiang
• Wang, Xiaojie
• Kee, Jia Xuan
• Yi, Fan
• Sun, Hongyan
• Yao, Shao Q.

Titel

Chemical Biology Tools for Protein Lysine Acylation

Ist Teil von

• Angewandte Chemie International Edition, 2022-05, Vol.61 (21), p.e202200303-n/a

Auflage

International ed. in English

Ort / Verlag

Germany: Wiley Subscription Services, Inc

Erscheinungsjahr

2022

Quelle

MEDLINE

Beschreibungen/Notizen

• 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. Chemical biology tools have emerged as a highly significant and promising means to investigate lysine post‐translational modifications (PTMs). This Review discusses different strategies using chemical biology probes to study lysine acylation and related regulatory proteins. Solutions to overcome problems in existing systems and future research directions are also proposed.