{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Weng W"],"funding":["National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["530-545"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11894137"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["32(3)"],"pubmed_abstract":["Lactates accumulation following traumatic brain injury (TBI) is detrimental. However, whether lactylation is triggered and involved in the deterioration of TBI remains unknown. Here, we first report that Tufm lactylation pathway induces neuronal apoptosis in TBI. Lactylation is found significantly increased in brain tissues from patients with TBI and mice with controlled cortical impact (CCI), and in neuronal injury cell models. Tufm, a key factor in mitophagy, is screened and identified to be mostly lactylated. Tufm is detected to be lactylated at K286 and the lactylation inhibits the interaction of Tufm and Tomm40 on mitochondria. The mitochondrial distribution of Tufm is then inhibited. Consequently, Tufm-mediated mitophagy is suppressed while mitochondria-induced neuronal apoptosis is "],"journal":["Cell death and differentiation"],"pubmed_title":["Tufm lactylation regulates neuronal apoptosis by modulating mitophagy in traumatic brain injury."],"pmcid":["PMC11894137"],"funding_grant_id":["82401610","82371379"],"pubmed_authors":["Peng Y","Jiang J","Huang J","Weng W","Jiang G","Qi W","Ma Z","Han Y","Lin Y","Wang J","Feng J","He Z","Gu J","Wang W","Feng Q"],"additional_accession":[]},"is_claimable":false,"name":"Tufm lactylation regulates neuronal apoptosis by modulating mitophagy in traumatic brain injury.","description":"Lactates accumulation following traumatic brain injury (TBI) is detrimental. However, whether lactylation is triggered and involved in the deterioration of TBI remains unknown. Here, we first report that Tufm lactylation pathway induces neuronal apoptosis in TBI. Lactylation is found significantly increased in brain tissues from patients with TBI and mice with controlled cortical impact (CCI), and in neuronal injury cell models. Tufm, a key factor in mitophagy, is screened and identified to be mostly lactylated. Tufm is detected to be lactylated at K286 and the lactylation inhibits the interaction of Tufm and Tomm40 on mitochondria. The mitochondrial distribution of Tufm is then inhibited. Consequently, Tufm-mediated mitophagy is suppressed while mitochondria-induced neuronal apoptosis is ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Mar","modification":"2026-07-16T23:21:02.711Z","creation":"2026-07-12T03:11:15.898Z"},"accession":"S-EPMC11894137","cross_references":{"pubmed":["39496783"],"doi":["10.1038/s41418-024-01408-0"]}}