Starvation promotes histone lysine butyrylation in the liver of male but not female mice

Goudarzi, Afsaneh; Hosseinmardi, Narges; Salami, Siamak; Mehdikhani, Fatemeh; Derakhshan, Samira; Aminishakib, Pouyan

doi:10.1016/j.gene.2020.144647

Cited by 9 publications

(8 citation statements)

References 30 publications

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“…Nevertheless, it was demonstrated that H3K9 butyrylation in human cells and mouse hearts is most enriched in mice fed a fat-free rather than high-fat diet, revealing the negative correlation with high-fat diets [ 35 ]. Interestingly, diet-related butyrylation was demonstrated to be sex-dependent, with starvation promoting the butyrylation of histone lysine in the liver cells in a gender-selective manner (only detected in males) [ 36 ]. Thus, increased histone butyrylation during starvation reinforces the concept of histone modification, linking the interaction between metabolism and epigenetics.…”

Section: The Identification and Characterization Of Novel Acylationmentioning

confidence: 99%

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

Shi,

Cui,

Qin

et al. 2024

Cell. Mol. Life Sci.

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Metastatic cancer is a major cause of cancer-related mortality; however, the complex regulation process remains to be further elucidated. A large amount of preliminary investigations focus on the role of epigenetic mechanisms in cancer metastasis. Notably, the posttranslational modifications were found to be critically involved in malignancy, thus attracting considerable attention. Beyond acetylation, novel forms of acylation have been recently identified following advances in mass spectrometry, proteomics technologies, and bioinformatics, such as propionylation, butyrylation, malonylation, succinylation, crotonylation, 2-hydroxyisobutyrylation, lactylation, among others. These novel acylations play pivotal roles in regulating different aspects of energy mechanism and mediating signal transduction by covalently modifying histone or nonhistone proteins. Furthermore, these acylations and their modifying enzymes show promise regarding the diagnosis and treatment of tumors, especially tumor metastasis. Here, we comprehensively review the identification and characterization of 11 novel acylations, and the corresponding modifying enzymes, highlighting their significance for tumor metastasis. We also focus on their potential application as clinical therapeutic targets and diagnostic predictors, discussing the current obstacles and future research prospects.

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Section: The Identification and Characterization Of Novel Acylationmentioning

confidence: 99%

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

Shi,

Cui,

Qin

et al. 2024

Cell. Mol. Life Sci.

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“…Further studies identified high levels of histone Kbu in intestinal epithelial cells from the cecum and distal mouse intestine (Gates et al., 2022). More in‐depth studies report the relative changes of Kbu in different physiological states; starvation enhances histone Kbu in the liver of males, though the basal levels of Kbu is higher in female mice (Goudarzi et al., 2020). Additionally, Kbu levels seem to be sensitive to dietary conditions in liver.…”

Section: Overview Of New Lysine Acylation Biomarkersmentioning

confidence: 99%

“…Additionally, Kbu levels seem to be sensitive to dietary conditions in liver. One study reported an increase in histone Kbu after the ketogenesis stimulation followed by starvation in liver (Goudarzi et al., 2020). However, H3K18bu levels were downregulated in a high‐fat diet‐induced obesity model (Nie et al., 2017).…”

Section: Overview Of New Lysine Acylation Biomarkersmentioning

confidence: 99%

New Histone Lysine Acylation Biomarkers and Their Roles in Epigenetic Regulation

Cat

Zheng

2023

Current Protocols

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Protein posttranslational modification (PTM) is a biochemical mechanism benefitting cellular adaptation to dynamic intracellular and environmental conditions. Recently, several acylation marks have been identified as new protein PTMs occurring on specific lysine residues in mammalian cells: isobutyrylation, methacrylation, benzoylation, isonicotinylation, and lactylation. These acylation marks were initially discovered to occur on nucleosomal histones, but they potentially occur as prevalent biomarkers on non-histone proteins as well. The existence of these PTMs is a downstream consequence of metabolism and demonstrates the intimate crosstalk between active cellular metabolites and regulation of protein function. Emerging evidence indicates that these acylation marks on histones affect DNA transcription and are functionally distinct from the well-studied lysine acetylation. Herein, we discuss enzymatic regulation and metabolic etiology of these acylations, 'reader' proteins that recognize different acylations, and their possible physiological and pathological functions. Several of these modifications correlate with other well-studied acylations and fine-tune the regulation of gene expression. Overall, findings of these acylation marks reveal new molecular links between metabolism and epigenetics and open up many questions for future investigation.

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“…ChIPseq and RNA-seq analyses have demonstrated that Kbhb in H3K9 is an active gene mark under conditions of starvation or STZ-induced diabetic ketosis and associated with genes upregulated in starvation-responsive metabolic pathways (e.g., amino acid catabolism, circadian rhythm, redox balance, PPAR signaling pathway, and insulin signaling pathway) [25]. There is a study providing evidence that the stimulation of ketogenesis following starvation leads to an increase in Kbhb and Kbu [62]. Similarly, Du et al [10] observed that increased malonylated proteins in both ob/ob and db/db diabetic mouse models, particularly in liver tissue, affected glucose and fatty acid metabolic pathways and reversed insulin resistance.…”

Section: The Dysregulation Of Novel Hptms Take Part In the Pathophysiology Of Diseasesmentioning

confidence: 99%

Function and Mechanism of Novel Histone Posttranslational Modifications in Health and Disease

et al. 2021

BioMed Research International

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Histone posttranslational modifications (HPTMs) are crucial epigenetic mechanisms regulating various biological events. Different types of HPTMs characterize and shape functional chromatin states alone or in combination, and dedicated effector proteins selectively recognize these modifications for gene expression. The dysregulation of HPTM recognition events takes part in human diseases. With the application of mass spectrometry- (MS-) based proteomics, novel histone lysine acylation has been successively discovered, e.g., propionylation, butyrylation, 2-hydroxyisobutyrylation, β-hydroxybutyrylation, malonylation, succinylation, crotonylation, glutarylation, and lactylation. These nine types of modifications expand the repertoire of HPTMs and regulate chromatin remodeling, gene expression, cell cycle, and cellular metabolism. Recent researches show that HPTMs have a close connection with the pathogenesis of cancer, metabolic diseases, neuropsychiatric disorders, infertility, kidney diseases, and acquired immunodeficiency syndrome (AIDS). This review focuses on the chemical structure, sites, functions of these novel HPTMs, and underlying mechanism in gene expression, providing a glimpse into their complex regulation in health and disease.

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Starvation promotes histone lysine butyrylation in the liver of male but not female mice

Cited by 9 publications

References 30 publications

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

A glimpse into novel acylations and their emerging role in regulating cancer metastasis

New Histone Lysine Acylation Biomarkers and Their Roles in Epigenetic Regulation

Function and Mechanism of Novel Histone Posttranslational Modifications in Health and Disease

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