Functions and mechanisms of lysine crotonylation

Wan, Junhu; Li, Hongyang; Chu, Jie; Zhang, Hongquan

doi:10.1111/jcmm.14650

Cited by 99 publications

(66 citation statements)

References 56 publications

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“…Notably, modifications to isobaric labeling improved its efficiency so that it requires significantly less reagent. The significant reduction in the cost per acquisition make it more likely that TMT will be adopted in clinical tests or patient-specific oncological mapping [52].…”

Section: Advanced Isotope Labeling Strategiesmentioning

confidence: 99%

“…As these advances make PTM-centric experiments easier, efforts to describe the biomedical causes and consequences of protein modifications are increasing. For example, recent applications of PTM-centric mass spectrometry studies include the acetylome effects of deacetylase SIRT5, implicated in maintaining mitochondrial function during acute kidney injury [69]; malonylation and crotonylation have functions in inflammatory signaling [70] and regulation of chromatin remodeling [52], respectively.…”

Section: Post-translational Modificationsmentioning

confidence: 99%

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Emerging mass spectrometry-based proteomics methodologies for novel biomedical applications

Pino

Rose

O’Broin

et al. 2020

Biochemical Society Transactions

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Research into the basic biology of human health and disease, as well as translational human research and clinical applications, all benefit from the growing accessibility and versatility of mass spectrometry (MS)-based proteomics. Although once limited in throughput and sensitivity, proteomic studies have quickly grown in scope and scale over the last decade due to significant advances in instrumentation, computational approaches, and bio-sample preparation. Here, we review these latest developments in MS and highlight how these techniques are used to study the mechanisms, diagnosis, and treatment of human diseases. We first describe recent groundbreaking technological advancements for MS-based proteomics, including novel data acquisition techniques and protein quantification approaches. Next, we describe innovations that enable the unprecedented depth of coverage in protein signaling and spatiotemporal protein distributions, including studies of post-translational modifications, protein turnover, and single-cell proteomics. Finally, we explore new workflows to investigate protein complexes and structures, and we present new approaches for protein–protein interaction studies and intact protein or top-down MS. While these approaches are only recently incipient, we anticipate that their use in biomedical MS proteomics research will offer actionable discoveries for the improvement of human health.

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Section: Advanced Isotope Labeling Strategiesmentioning

confidence: 99%

Section: Post-translational Modificationsmentioning

confidence: 99%

Emerging mass spectrometry-based proteomics methodologies for novel biomedical applications

Pino

Rose

O’Broin

et al. 2020

Biochemical Society Transactions

View full text Add to dashboard Cite

show abstract

“…Gene Ontology (GO) annotation proteome was derived from the UniProt-GOA The CREBBP and p300 proteins as well as PCAF and MOF catalyze the crotonylation on histones and non-histone proteins 3 . Crotonylation has been demonstrated to be involved transcription and DNA repair 3,4 . Though several proteomic studies have been focused on the regulation of crotonylation in cells [4][5][6] (1.5~2) and Q4 (>2).…”

Section: Bioinformatics Analysismentioning

confidence: 99%

Global profiling of the crotonylome in Small Cell Lung Cancer

Guo

Huang

et al. 2020

Preprint

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AbstractSmall cell lung cancer is a deadly neuroendocrine lung cancer subtype, which harbors the driver mutations of RB1 and TP53 as well as EP300/CREBBP. Since CREBBP/p300 are two prominent crotonyl-CoA transferases responsible for the global crotonylation in cells, here we investigated the crotonylome in SCLC tissues compared with normal lung tissues through TMT labeling coupled with LC-MS/MS and found unique patterns of protein crotonylation in SCLC related pathways.

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“…These observations support the notion that protein crotonylation may be functionally important for maintaining cell identity in these different culture conditions. In this regard, protein crotonylation is controlled by the balance between writers and erasers [25], whose changes in expression could explain putative differences in crotonylation between the four cell states. However, analysis of the total proteome showed that known crotonylation writers and erasers (also crotonylation readers) do not change noticeably between the four cell states ( Figure S1E).…”

Section: Quantitative Lysine Crotonylome Analysis In Different Pluripmentioning

confidence: 99%

Global Profiling of the Lysine Crotonylome in Different Pluripotent States

Meng

et al. 2020

Preprint

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Pluripotent stem cells (PSCs) can be expanded in vitro in different culture conditions, resulting in a spectrum of cell states with distinct properties. Understanding how PSCs transition from one state to another, ultimately leading to lineage-specific differentiation, is important for developmental biology and regenerative medicine. Although there is significant information regarding gene expression changes controlling these transitions, less is known about post-translational modifications of proteins. Protein crotonylation is a newly discovered post-translational modification where lysine residues are modified with a crotonyl group. Here, we employed affinity purification of crotonylated peptides and liquid chromatography-tandem mass spectrometry (LC-MS/MS) to systematically profile protein crotonylation in mouse PSCs in different states including ground, metastable and primed state, as well as metastable PSCs undergoing early pluripotency exit. We successfully identified 3628 high-confidence sites in 1426 proteins. These crotonylated proteins are enriched for factors involved in functions related to pluripotency such as RNA biogenesis, central carbon metabolism and proteasome function. Moreover, we found that increasing the cellular levels of crotonyl-CoA through crotonic acid treatment promotes proteasome activity in metastable PSCs and delays their differentiation, consistent with previous observations showing that enhanced proteasomal activity helps to sustain pluripotency. Our atlas of protein crotonylation will be valuable for further studies of pluripotency regulation and may also provide insights into the role of metabolism in other cell fate transitions.

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Functions and mechanisms of lysine crotonylation

Cited by 99 publications

References 56 publications

Emerging mass spectrometry-based proteomics methodologies for novel biomedical applications

Emerging mass spectrometry-based proteomics methodologies for novel biomedical applications

Global profiling of the crotonylome in Small Cell Lung Cancer

Global Profiling of the Lysine Crotonylome in Different Pluripotent States

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