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@ARTICLE{Vercellino:1038811,
      author       = {Vercellino, Irene and Sazanov, Leonid A.},
      title        = {{SCAF}1 drives the compositional diversity of mammalian
                      respirasomes},
      journal      = {Biochimica et biophysica acta / Bioenergetics},
      volume       = {1865},
      issn         = {0005-2728},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2025-01648},
      pages        = {149113 -},
      year         = {2024},
      abstract     = {The ATP synthase in themitochondria of each human being
                      generatesabout 50 kg of ATP daily, maintaining a steady
                      state level of about 10 g tosustain life. The enzyme has a
                      rotarymechanism to transmit energy froma transmembrane
                      proton motive force across the inner membrane of
                      theorganelle (derived by respiration) to the catalytic sites
                      where ATP isformed from ADP and phosphate. The bovine enzyme
                      is made of 29protein subunits of 18 types, including the
                      inhibitor protein IF1 [1,2]. Theyare organised into a rotor
                      and a stator. The rotor consists of a membranebound c8-ring
                      attached to a central stalk (subunits γ, δ and ε)
                      thatprotrudes into the mitochondrialmatrix, and penetrates
                      into the sphericalcatalytic domain (α3β3) of the stator.
                      The stator is completed by aperipheral stalk (PS; subunits
                      OSCP, F6, b and d), bound to the externalsurface of the
                      catalytic domain and extending into themembrane
                      domain(subunits ATP6 and ATP8 plus three small membrane
                      subunits e, f and g,which form a wedge encapsulating lipid
                      molecules). ATP6 is intimatelyassociated with the c8-ring
                      and provides two proton half channelsinvolved in the
                      generation of rotation. The wedges in two ATP
                      synthasesinteract to formthe characteristic dimers that sit
                      on the tips of the cristaeand subunit k links dimers
                      together. The assembly of the human enzymeinvolves the
                      formation of intermediate modules representing (i)
                      thecatalytic domain (α3β3γδε, or F1, plus IF1), (ii)
                      the PS plus the membrane"wedge". [3,4], and (iii)
                      themembrane bound c8-rotor ring [5]. They formthe key
                      intermediate F1-IF1-c8-PS [5] into which subunits ATP6 and
                      ATP8are inserted between the c8-ring and the wedge with
                      subunit j bound toATP6, forming the proton pathway. Two
                      protein assembly factors arerequired to build the c8-ring
                      and three others to assemble the catalyticdomain. IF1 is
                      another key assembly factor that intervenes to
                      preventpartially formed complexes that are capable of ATP
                      hydrolysis (but notsynthesis) from doing so. The assembly
                      pathway reflects the probablemodular path of evolution of
                      the enzyme. Finally, I will comment on thelack of
                      involvement of ATP synthase in the permeability transition.},
      cin          = {ER-C-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ER-C-3-20170113},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:001311206700011},
      doi          = {10.1016/j.bbabio.2024.149113},
      url          = {https://juser.fz-juelich.de/record/1038811},
}