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| 001 | 279442 | ||
| 005 | 20250720001551.0 | ||
| 024 | 7 | _ | |a 10.1016/j.molcel.2025.05.036 |2 doi |
| 024 | 7 | _ | |a pmid:40578348 |2 pmid |
| 024 | 7 | _ | |a 1097-2765 |2 ISSN |
| 024 | 7 | _ | |a 1097-4164 |2 ISSN |
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| 037 | _ | _ | |a DZNE-2025-00773 |
| 041 | _ | _ | |a English |
| 082 | _ | _ | |a 610 |
| 100 | 1 | _ | |a Rothemann, Robin Alexander |b 0 |
| 245 | _ | _ | |a Interaction with AK2A links AIFM1 to cellular energy metabolism. |
| 260 | _ | _ | |a [Cambridge, Mass.] |c 2025 |b Cell Press |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a 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, in the case of MIA40, affecting the cofactor-binding site. The AIFM1-AK2A interaction is important during mitochondrial respiration because AIFM1 serves as a recruiting hub within the IMS, regulating mitochondrial bioenergetic output by creating hotspots of metabolic enzymes. |
| 536 | _ | _ | |a 351 - Brain Function (POF4-351) |0 G:(DE-HGF)POF4-351 |c POF4-351 |f POF IV |x 0 |
| 536 | _ | _ | |a 352 - Disease Mechanisms (POF4-352) |0 G:(DE-HGF)POF4-352 |c POF4-352 |f POF IV |x 1 |
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| 650 | _ | 7 | |a AIFM1 |2 Other |
| 650 | _ | 7 | |a AK2 |2 Other |
| 650 | _ | 7 | |a ATP |2 Other |
| 650 | _ | 7 | |a ATP transport |2 Other |
| 650 | _ | 7 | |a MIA40/CHCHD4 |2 Other |
| 650 | _ | 7 | |a MICOS |2 Other |
| 650 | _ | 7 | |a metabolism |2 Other |
| 650 | _ | 7 | |a mitochondria |2 Other |
| 700 | 1 | _ | |a Pavlenko, Egor |b 1 |
| 700 | 1 | _ | |a Mondal, Mrityunjoy |0 P:(DE-2719)9001754 |b 2 |u dzne |
| 700 | 1 | _ | |a Gerlich, Sarah |b 3 |
| 700 | 1 | _ | |a Grobushkin, Pavel |b 4 |
| 700 | 1 | _ | |a Mostert, Sebastian |b 5 |
| 700 | 1 | _ | |a Racho, Julia |b 6 |
| 700 | 1 | _ | |a Weiss, Konstantin |b 7 |
| 700 | 1 | _ | |a Stobbe, Dylan |b 8 |
| 700 | 1 | _ | |a Stillger, Katharina |b 9 |
| 700 | 1 | _ | |a Lapacz, Kim |b 10 |
| 700 | 1 | _ | |a Salscheider, Silja Lucia |b 11 |
| 700 | 1 | _ | |a Petrungaro, Carmelina |b 12 |
| 700 | 1 | _ | |a Ehninger, Dan |0 P:(DE-2719)2289209 |b 13 |u dzne |
| 700 | 1 | _ | |a Nguyen, Thi Hoang Duong |b 14 |
| 700 | 1 | _ | |a Dengjel, Jörn |b 15 |
| 700 | 1 | _ | |a Neundorf, Ines |b 16 |
| 700 | 1 | _ | |a Bano, Daniele |0 P:(DE-2719)2158358 |b 17 |u dzne |
| 700 | 1 | _ | |a Poepsel, Simon |b 18 |
| 700 | 1 | _ | |a Riemer, Jan |b 19 |
| 773 | _ | _ | |a 10.1016/j.molcel.2025.05.036 |g p. S1097276525005003 |0 PERI:(DE-600)2001948-8 |n 13 |p 2550 - 2566.e6 |t Molecular cell |v 85 |y 2025 |x 1097-2765 |
| 856 | 4 | _ | |u https://pub.dzne.de/record/279442/files/DZNE-2025-00773%20SUP.zip |
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