Proteomics

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Global profiling of protein lactylation in Caenorhabditis elegans (label-free quantitative proteomic data)

ABSTRACT: We identified 1836 Class I (locnalization probabilities > 0.75) lactylated sites in 487 proteis,This study establish the first lactylome database in Caenorhabditis elegans and provides a basis for studying the role of lactylation. In addition, it provides a evidence for the existence of lactylation of non-histones and their possible involvement in biological processes.

ORGANISM(S): Caenorhabditis Elegans

SUBMITTER: Juntao Yang  

PROVIDER: PXD041277 | iProX | Thu Mar 30 00:00:00 BST 2023

REPOSITORIES: iProX

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Publications

Global profiling of protein lactylation in Caenorhabditis elegans.

Ding Tao T   Yang Ye-Hong YH   Wang Qiao-Chu QC   Wu Yue Y   Han Rong R   Zhang Xu-Tong XT   Kong Jie J   Yang Jun-Tao JT   Liu Jiang-Feng JF  

Proteomics 20231017 1-2

Lactylation, as a novel posttranslational modification, is essential for studying the functions and regulation of proteins in physiological and pathological processes, as well as for gaining in-depth knowledge on the occurrence and development of many diseases, including tumors. However, few studies have examined the protein lactylation of one whole organism. Thus, we studied the lactylation of global proteins in Caenorhabditis elegans to obtain an in vivo lactylome. Using an MS-based platform,  ...[more]