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Crosstalk between crotonylation and other post-translational modifications: Enlightening a promising avenue in disease regulation
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DOI：10.1016/j.gendis.2026.102390.png)
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Abstract
En 中文
Proteins undergo one or more distinct types of post-translational modification (PTM) in an orchestrated manner to collectively influence protein functions. Crotonylation is a newly identified PTM that may regulate cellular processes and disease progression. Although multitudinous scientific reports on crotonylation have been published in recent years, knowledge gaps concerning the crosstalk between crotonylation and other PTMs in disease development remain. Furthermore, to date, selective methods for PTM crosstalk analysis remain limited. The development of new techniques to study this PTM crosstalk will hopefully accelerate the development of new therapeutics for diseases. In this review, we briefly review protein crotonylation, which occurs on histone and non-histone proteins, and summarize the regulatory factors involved in this modification. Moreover, we aim to provide a comprehensive and critical evaluation of the crosstalk between protein crotonylation and other PTMs, including phosphorylation, ubiquitylation, acetylation, lactylation, succinylation, and 2-hydroxyisobutyrylation. Meanwhile, this review focuses on their impact on disease pathogenesis. Finally, we focus on current methodologies for identifying PTM crosstalk. Overall, this review aims to deepen the understanding of the relationship between protein crotonylation and other PTMs and to inspire future studies and therapeutic innovation.
Keywords:
Crosstalk
Crotonylation
Detection Methods
Diseases regulation
Post-translational modifications
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