{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["85(13)"],"submitter":["Rothemann RA"],"pubmed_abstract":["Apoptosis-inducing factor 1 (AIFM1) is a flavoprotein essential for mitochondrial function and biogenesis. Its interaction with MIA40/CHCHD4, the central component of the mitochondrial disulfide relay, accounts for some, but not all, aspects of AIFM1 function. We provide a high-confidence AIFM1 interactome that elucidates functional partners within the mitochondrial intermembrane space. We found that AIFM1 binding to adenylate kinase 2 (AK2), an essential enzyme that maintains cellular adenine nucleotide pools, depends on the AK2 C-terminal domain. High-resolution cryoelectron microscopy (cryo-EM) and biochemical analyses showed that both MIA40 and AK2A bind the AIFM1 C-terminal β-sheet domain. Their binding enhances NADH oxidoreductase activity by locking an active dimer conformation and,"],"journal":["Molecular cell"],"pagination":["2550-2566.e6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617965"],"repository":["biostudies-literature"],"pubmed_title":["Interaction with AK2A links AIFM1 to cellular energy metabolism."],"pmcid":["PMC7617965"],"pubmed_authors":["Riemer J","Mondal M","Stillger K","Petrungaro C","Stobbe D","Nguyen THD","Mostert S","Racho J","Rothemann RA","Bano D","Gerlich S","Ehninger D","Lapacz K","Weiss K","Neundorf I","Salscheider SL","Dengjel J","Grobushkin P","Poepsel S","Pavlenko E"],"additional_accession":[]},"is_claimable":false,"name":"Interaction with AK2A links AIFM1 to cellular energy metabolism.","description":"Apoptosis-inducing factor 1 (AIFM1) is a flavoprotein essential for mitochondrial function and biogenesis. Its interaction with MIA40/CHCHD4, the central component of the mitochondrial disulfide relay, accounts for some, but not all, aspects of AIFM1 function. We provide a high-confidence AIFM1 interactome that elucidates functional partners within the mitochondrial intermembrane space. We found that AIFM1 binding to adenylate kinase 2 (AK2), an essential enzyme that maintains cellular adenine nucleotide pools, depends on the AK2 C-terminal domain. High-resolution cryoelectron microscopy (cryo-EM) and biochemical analyses showed that both MIA40 and AK2A bind the AIFM1 C-terminal β-sheet domain. Their binding enhances NADH oxidoreductase activity by locking an active dimer conformation and,","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-03-31T10:36:54.812Z","creation":"2025-08-24T03:06:55.162Z"},"accession":"S-EPMC7617965","cross_references":{"pubmed":["40578348"],"doi":["10.1016/j.molcel.2025.05.036"]}}