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@ARTICLE{Rothemann:279442,
      author       = {Rothemann, Robin Alexander and Pavlenko, Egor and Mondal,
                      Mrityunjoy and Gerlich, Sarah and Grobushkin, Pavel and
                      Mostert, Sebastian and Racho, Julia and Weiss, Konstantin
                      and Stobbe, Dylan and Stillger, Katharina and Lapacz, Kim
                      and Salscheider, Silja Lucia and Petrungaro, Carmelina and
                      Ehninger, Dan and Nguyen, Thi Hoang Duong and Dengjel, Jörn
                      and Neundorf, Ines and Bano, Daniele and Poepsel, Simon and
                      Riemer, Jan},
      title        = {{I}nteraction with {AK}2{A} links {AIFM}1 to cellular
                      energy metabolism.},
      journal      = {Molecular cell},
      volume       = {85},
      number       = {13},
      issn         = {1097-2765},
      address      = {[Cambridge, Mass.]},
      publisher    = {Cell Press},
      reportid     = {DZNE-2025-00773},
      pages        = {2550 - 2566.e6},
      year         = {2025},
      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, 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.},
      keywords     = {AIFM1 (Other) / AK2 (Other) / ATP (Other) / ATP transport
                      (Other) / MIA40/CHCHD4 (Other) / MICOS (Other) / metabolism
                      (Other) / mitochondria (Other)},
      cin          = {AG Bano / AG Ehninger},
      ddc          = {610},
      cid          = {I:(DE-2719)1013003 / I:(DE-2719)1013005},
      pnm          = {351 - Brain Function (POF4-351) / 352 - Disease Mechanisms
                      (POF4-352)},
      pid          = {G:(DE-HGF)POF4-351 / G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40578348},
      doi          = {10.1016/j.molcel.2025.05.036},
      url          = {https://pub.dzne.de/record/279442},
}