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Article

Crotonylation impedes c-Myc oncogenic activity.

Proceedings of the National Academy of Sciences of the United States of America - 9 Jun 2026

Wallbillich Nicholas J, Liao Peng, Srivastava Rashmi, Fan Jia, Zeng Shelya X, Lu Hua

Abstract excerpt

c-Myc, an important oncoprotein, is highly regulated via posttranslational modifications. Herein, we report c-Myc crotonylation, an acylation stemming from the short-chain fatty acid crotonate. By biochemical analyses and high-resolution mass spectrometry sequencing, we showed that c-Myc is crotonylated at several lysine residues, spanning its middle to C termini. Mutation of these crotonylation sites conferred...

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Share to Acylation
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Proto-Oncogene Proteins c-myc

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Source

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Identifiers

PMID: 42224600
DOI: 10.1073/pnas.2530020123
PMCID: PMC13250510

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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