Protein crotonylation: Basic research and clinical diseases

Li, Dongling; Lin, Ling; Xu, Fan; Feng, Tianlin; Tao, Yang; Miao, Hongming; Yang, Fan

doi:10.1016/j.bbrep.2024.101694

Biochemistry and Biophysics Reports

2024

DOI: 10.1016/j.bbrep.2024.101694

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Protein crotonylation: Basic research and clinical diseases

Dongling Li,

Ling Lin,

Fan Xu

et al.

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2024

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Cited by 2 publications

References 114 publications

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Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification

Westerveld,

Besermenji,

Aidukas

et al. 2024

ChemBioChem

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Lysine crotonylation (Kcr) is a recently discovered post‐translational modification (PTM). Both histone and non‐histone Kcr‐proteins have been associated with numerous diseases including cancer, acute kidney injury, HIV latency, and cardiovascular disease. Histone Kcr enhances gene expression to a larger extend than the extensively studied lysine acetylation (Kac), suggesting Kcr as a novel potential therapeutic target. Although numerous scientific reports on crotonylation were published in the last years, relevant knowledge gaps concerning this PTM and its regulation still remain. To date, only few selective Kcr‐interacting proteins have been identified and selective methods for the enrichment of Kcr‐proteins in chemical proteomics analysis are still lacking. The development of new techniques to study this underexplored PTM could then clarify its function in health and disease and hopefully accelerate the development of new therapeutics for Kcr‐related disease. Herein we briefly review what is known about the regulation mechanisms of Kcr and the current methods used to identify Kcr‐proteins and their interacting partners. This report aims to highlight the significant potential of Kcr as a therapeutic target and to identify the existing scientific gaps that new research must address.

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Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification

Westerveld,

Besermenji,

Aidukas

et al. 2024

ChemBioChem

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Regulatory Mechanism of Protein Crotonylation and Its Relationship with Cancer

Yang,

Fan,

2024

Cells

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Crotonylation is a recently discovered protein acyl modification that shares many enzymes with acetylation. However, it possesses a distinct regulatory mechanism and biological function due to its unique crotonyl structure. Since the discovery of crotonylation in 2011, numerous crotonylation sites have been identified in both histones and other proteins. In recent studies, crotonylation was found to play a role in various diseases and biological processes. This paper reviews the initial discovery and regulatory mechanisms of crotonylation, including various writer, reader, and eraser proteins. Finally, we emphasize the relationship of dysregulated protein crotonylation with eight common malignancies, including cervical, prostate, liver, and lung cancer, providing new potential therapeutic targets.

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Protein crotonylation: Basic research and clinical diseases

Cited by 2 publications

References 114 publications

Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification

Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post‐Translational Modification

Regulatory Mechanism of Protein Crotonylation and Its Relationship with Cancer

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