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@ARTICLE{Schirmeyer:894207,
      author       = {Schirmeyer, Jana and Hummert, Sabine and Eick, Thomas and
                      Schulz, Eckhard and Schwabe, Tina and Ehrlich, Gunter and
                      Kukaj, Taulant and Wiegand, Melanie and Sattler, Christian
                      and Schmauder, Ralf and Zimmer, Thomas and Kosmalla, Nisa
                      and Münch, Jan and Bonus, Michele and Gohlke, Holger and
                      Benndorf, Klaus},
      title        = {{T}hermodynamic profile of mutual subunit control in a
                      heteromeric receptor},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {118},
      number       = {30},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2021-03098},
      pages        = {e2100469118},
      year         = {2021},
      abstract     = {Cyclic nucleotide-gated (CNG) ion channels of olfactory
                      neurons are tetrameric membrane receptors that are composed
                      of two A2 subunits, one A4 subunit, and one B1b subunit.
                      Each subunit carries a cyclic nucleotide-binding domain in
                      the carboxyl terminus, and the channels are activated by the
                      binding of cyclic nucleotides. The mechanism of cooperative
                      channel activation is still elusive. Using a complete set of
                      engineered concatenated olfactory CNG channels, with all
                      combinations of disabled binding sites and fit analyses with
                      systems of allosteric models, the thermodynamics of
                      microscopic cooperativity for ligand binding was subunit-
                      and state-specifically quantified. We show, for the closed
                      channel, that preoccupation of each of the single subunits
                      increases the affinity of each other subunit with a Gibbs
                      free energy (ΔΔG) of ∼−3.5 to ∼−5.5 kJ ⋅
                      mol−1, depending on the subunit type, with the only
                      exception that a preoccupied opposite A2 subunit has no
                      effect on the other A2 subunit. Preoccupation of two
                      neighbor subunits of a given subunit causes the maximum
                      affinity increase with ΔΔG of ∼−9.6 to ∼−9.9 kJ
                      ⋅ mol−1. Surprisingly, triple preoccupation leads to
                      fewer negative ΔΔG values for a given subunit as compared
                      to double preoccupation. Channel opening increases the
                      affinity of all subunits. The equilibrium constants of
                      closed–open isomerizations systematically increase with
                      progressive liganding. This work demonstrates, on the
                      example of the heterotetrameric olfactory CNG channel, a
                      strategy to derive detailed insights into the specific
                      mutual control of the individual subunits in a multisubunit
                      membrane receptor.},
      cin          = {JSC / NIC / IBI-7 / IBG-4},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JSC-20090406 / I:(DE-Juel1)NIC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBG-4-20200403},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217) /
                      2172 - Utilization of renewable carbon and energy sources
                      and engineering of ecosystem functions (POF4-217) /
                      Forschergruppe Gohlke $(hkf7_20200501)$},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
                      G:(DE-HGF)POF4-2172 / $G:(DE-Juel1)hkf7_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {34301910},
      UT           = {WOS:000685039000028},
      doi          = {10.1073/pnas.2100469118},
      url          = {https://juser.fz-juelich.de/record/894207},
}