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@ARTICLE{Krner:848280,
      author       = {Körner, Jannis and Meents, Jannis and Machtens,
                      Jan-Philipp and Lampert, Angelika},
      title        = {β1 subunit stabilises sodium channel {N}av1.7 against
                      mechanical stress},
      journal      = {The journal of physiology},
      volume       = {596},
      number       = {12},
      issn         = {0022-3751},
      address      = {Hoboken, NJ},
      publisher    = {Wiley-Blackwell},
      reportid     = {FZJ-2018-03541},
      pages        = {2433-2445},
      year         = {2018},
      abstract     = {Voltage‐gated sodium channels are key players in neuronal
                      excitability and pain signalling. Precise gating of these
                      channels is crucial as even small functional alterations can
                      lead to pathological phenotypes such as pain or heart
                      failure. Mechanical stress has been shown to affect sodium
                      channel activation and inactivation. This suggests that
                      stabilising components are necessary to ensure precise
                      channel gating in living organisms. Here, we show that
                      mechanical shear stress affects voltage dependence of
                      activation and fast inactivation of the Nav1.7 channel.
                      Co‐expression of the β1 subunit, however, protects both
                      gating modes of Nav1.7 against mechanical shear stress.
                      Using molecular dynamics simulation, homology modelling and
                      site‐directed mutagenesis, we identify an intramolecular
                      disulfide bond of β1 (Cys21‐Cys43) which is partially
                      involved in this process: the β1‐C43A mutant prevents
                      mechanical modulation of voltage dependence of activation,
                      but not of fast inactivation. Our data emphasise the unique
                      role of segment 6 of domain IV for sodium channel fast
                      inactivation and confirm previous reports that the
                      intracellular process of fast inactivation can be modified
                      by interfering with the extracellular end of segment 6 of
                      domain IV. Thus, our data suggest that physiological gating
                      of Nav1.7 may be protected against mechanical stress in a
                      living organism by assembly with the β1 subunit.},
      cin          = {ICS-4 / JARA-HPC},
      ddc          = {610},
      cid          = {I:(DE-Juel1)ICS-4-20110106 / $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      MOLECULAR MODELLING OF BIFUNCTIONAL MEMBRANE TRANSPORT
                      PROTEINS $(jics40_20130501)$ / Mechanisms of Ca2+-activated
                      Cl- channels and lipid scramblases of the TMEM16 family
                      $(jics41_20161101)$ / Multiscale simulations of
                      voltage-gated sodium channel complexes and clusters
                      $(jics42_20181101)$},
      pid          = {G:(DE-HGF)POF3-551 / $G:(DE-Juel1)jics40_20130501$ /
                      $G:(DE-Juel1)jics41_20161101$ /
                      $G:(DE-Juel1)jics42_20181101$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29659026},
      UT           = {WOS:000435286000016},
      doi          = {10.1113/JP275905},
      url          = {https://juser.fz-juelich.de/record/848280},
}