Cysteine post-translational modifications: ten years from chemical proteomics to bioinformatics

TL;DR

This paper reviews a decade of advances in detecting and predicting cysteine post-translational modifications, highlighting technological progress and bioinformatics approaches to understanding their biological roles.

Contribution

It provides a comprehensive summary of cysteine PTM identification methods and discusses in silico prediction strategies, guiding future research directions.

Findings

Advances in chemical proteomics have improved cysteine PTM detection.

Bioinformatics tools are increasingly effective for predicting cysteine modifications.

Cysteine PTMs are crucial for regulating protein functions and interactions.

Abstract

As the only thiol-bearing amino acid, cysteine (Cys) residues in proteins have the reactive thiol side chain, which is susceptible to a series of post-translational modifications (PTMs). These PTMs participate in a wide range of biological activities including the alteration of enzymatic reactions, protein-protein interactions and protein stability. Here we summarize the advance of cysteine PTM identification technologies and the features of the various kinds of the PTMs. We also discuss in silico approaches for the prediction of the different types of cysteine modified sites, giving directions for future study.