Dataset Information

Lactylation contributes to colorectal carcinogenesis

ABSTRACT: To reveal the lactylated proteins in CRC, we analyzed the lactyl-proteome from seven paired biopsies from CRC patients by using mass spectrometry analysis (LC-MS/MS). Meanwhile, we used LC-MS to identify Kla and Kac substrates upon HCT116 cells.

ORGANISM(S): Homo Sapiens

SUBMITTER: Bingteng Xie

PROVIDER: PXD037744 | iProX | Thu Oct 27 00:00:00 BST 2022

REPOSITORIES: iProX

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Publications

KAT8-catalyzed lactylation promotes eEF1A2-mediated protein synthesis and colorectal carcinogenesis.

Xie Bingteng B Zhang Mengdi M Li Jie J Cui Jianxin J Zhang Pengju P Liu Fangming F Wu Yuxi Y Deng Weiwei W Ma Jihong J Li Xinyu X Pan Bingchen B Zhang Baohui B Zhang Hongbing H Luo Aiqin A Xu Yinzhe Y Li Mo M Pu Yang Y

Proceedings of the National Academy of Sciences of the United States of America 20240215 8

Aberrant lysine lactylation (Kla) is associated with various diseases which are caused by excessive glycolysis metabolism. However, the regulatory molecules and downstream protein targets of Kla remain largely unclear. Here, we observed a global Kla abundance profile in colorectal cancer (CRC) that negatively correlates with prognosis. Among lactylated proteins detected in CRC, lactylation of eEF1A2K408 resulted in boosted translation elongation and enhanced protein synthesis which contributed t ...[more]

PMID: 38359291

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Project description:Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. Increasing evidence demonstrates that lysine lactylation plays an important regulatory role in metabolic processes in both bacterial and human cells. However, little is known about the extent and function of lysine lactylation in fungi, here investigated with the black yeast Phialophora verrucosaverrucose as a model organism. WeHere, we report the first proteomic survey of this modification in P. verrucosa. We performed a global lactylation analysis of P. verrucosa using high accuracy bottom-up nano-LC-MS/MS in combination wwith the enrichment of lactylated peptides from digested cell lysates and subsequent peptide identification. In total, 636 lactylation sites on 420 lactylated proteins were identified in this pathogen, of which contained in 26 types of modification motifs. Our results show that over 85% of lactylated proteins were distributed in cytoplasm, mitochondria, and nucleus. The identified proteins were found to be involved associated toin diverse biological processes and were significantly enriched in the melanin biosynthesis process. Most strikingly, Kla was found in 23 structural constituent proteins of ribosome, indicating an impact of Kla in protein synthesis . Moreover, 12 lactylated proteins participated in fungal pathogenicity, suggesting a potential role for Kla in this process. Protein interaction network analysis suggested that a mass of protein interactions are regulated by lactylation. Together, our findings reveal widespread roles for lysine lactylation in regulating metabolism and melanin biosynthesis in P. verrucosa. Our data provide a rich resource for functional analyses of lactylation and facilitate the dissection of metabolic networks in this pathogen. The combined data sets represent the first report of the lactylome of P. verrucosa and provide a good foundation for further explorations of Kla in clinical fungal pathogens.

Dataset Information

Lactylation contributes to colorectal carcinogenesis

Publications

KAT8-catalyzed lactylation promotes eEF1A2-mediated protein synthesis and colorectal carcinogenesis.

Similar Datasets

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