{"database":"iProX","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Yunzi Mao"],"species":["Homo Sapiens"],"full_dataset_link":["http://www.iprox.org/page/project.html?id=IPX0018359000"],"submitter_email":["maoyz@fudan.edu.cn"],"submitter_affiliation":["Fudan University"],"sample_protocol":[""],"repository":["iProX"],"data_protocol":[""],"additional_accession":[]},"is_claimable":false,"name":"ATRIP Lactylation Induces Cell Cycle Arrest Escape and Chemoresistance","description":"Elevated lactate levels were associated with chemoresistance across multiple cancer types. Mechanistically, lactylation of ATRIP at lysine 270 (Lac-K270) enhanced ATR-ATRIP interaction, resulting in aberrant ATR activation and subsequent checkpoint kinase 1 (CHK1) degradation via the ubiquitin-proteasome pathway. This rewired the ATR-CHK1 DDR pathway, enabling cancer cells to bypass chemotherapy-induced cell cycle arrest and survive genotoxic stress. Lac-K270 was catalyzed by alanyl-tRNA synthetase 1 (AARS1) and reversed by the deacetylase sirtuin 1 (SIRT1). Pharmacological inhibition of Lac-K270 with alaninol effectively re-sensitized chemoresistant tumors to genotoxic drugs in both in vitro and animal models.","dates":{"publication":"Tue Jul 21 00:00:00 GMT+01:00 2026"},"accession":"PXD081427","cross_references":{"TAXONOMY":["9606"]}}