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The Chemical Biology of Reversible Lysine Post-translational Modifications.

ABSTRACT: Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the "writers," "erasers," and "readers" of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologies, that have helped to delineate Lys PTM functions and show promise for a diverse set of biomedical applications.

SUBMITTER: Wang ZA

PROVIDER: S-EPMC7487139 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature

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The Chemical Biology of Reversible Lysine Post-translational Modifications.

Wang Zhipeng A ZA Cole Philip A PA

Cell chemical biology 20200721 8

Lysine (Lys) residues in proteins undergo a wide range of reversible post-translational modifications (PTMs), which can regulate enzyme activities, chromatin structure, protein-protein interactions, protein stability, and cellular localization. Here we discuss the "writers," "erasers," and "readers" of some of the common protein Lys PTMs and summarize examples of their major biological impacts. We also review chemical biology approaches, from small-molecule probes to protein chemistry technologi ...[more]

PMID: 32698016

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