{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Mussulini BHM"],"funding":["European Molecular Biology Organization","Fundacja na rzecz Nauki Polskiej","Fundacja na rzecz Nauki Polskiej (FNP)","Narodowe Centrum Nauki","European Molecular Biology Organization (EMBO)","Narodowe Centrum Nauki (NCN)"],"pagination":["1835-1862"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11976965"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(7)"],"pubmed_abstract":["Mitochondria harbor respiratory complexes that perform oxidative phosphorylation. Complex I is the first enzyme of the respiratory chain that oxidizes NADH. A dysfunction in complex I can result in higher cellular levels of NADH, which in turn strengthens the interaction between apoptosis-inducing factor 1 (AIFM1) and Mitochondrial intermembrane space import and assembly protein 40 (MIA40) in the mitochondrial intermembrane space. We investigated whether MIA40 modulates the activity of AIFM1 upon increased NADH/NAD+ balance. We found that in model cells characterized by an increase in NADH the AIFM1-MIA40 interaction is strengthened and these cells demonstrate resistance to AIFM1-induced cell death. Either silencing of MIA40, rescue of complex I, or depletion of NADH through the expression"],"journal":["EMBO reports"],"pubmed_title":["MIA40 suppresses cell death induced by apoptosis-inducing factor 1."],"pmcid":["PMC11976965"],"funding_grant_id":["ALTF 388-2023","2019/35/B/NZ3/04095","2019/33/B/NZ5/00780","2019/35/B/NZ3/04066","MAB/2017/2"],"pubmed_authors":["Ayyamperumal S","Wasilewski M","Chacinska A","Wnorowski A","Draczkowski P","Borrero-Landazabal MA","Mussulini BHM","Maruszczak KK"],"additional_accession":[]},"is_claimable":false,"name":"MIA40 suppresses cell death induced by apoptosis-inducing factor 1.","description":"Mitochondria harbor respiratory complexes that perform oxidative phosphorylation. Complex I is the first enzyme of the respiratory chain that oxidizes NADH. A dysfunction in complex I can result in higher cellular levels of NADH, which in turn strengthens the interaction between apoptosis-inducing factor 1 (AIFM1) and Mitochondrial intermembrane space import and assembly protein 40 (MIA40) in the mitochondrial intermembrane space. We investigated whether MIA40 modulates the activity of AIFM1 upon increased NADH/NAD+ balance. We found that in model cells characterized by an increase in NADH the AIFM1-MIA40 interaction is strengthened and these cells demonstrate resistance to AIFM1-induced cell death. Either silencing of MIA40, rescue of complex I, or depletion of NADH through the expression","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-07-15T11:01:47.529Z","creation":"2026-07-03T03:16:14.689Z"},"accession":"S-EPMC11976965","cross_references":{"pubmed":["40055465"],"doi":["10.1038/s44319-025-00406-8"]}}