% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Steinke:202863,
      author       = {Steinke, Kim Vanessa and Gorinski, Nataliya and
                      Wojciechowski, Daniel and Todorov, Vladimir and Guseva,
                      Daria and Ponimaskin, Evgeni and Fahlke, Christoph and
                      Fischer, Martin},
      title        = {{H}uman {CLC}-{K} {C}hannels {R}equire {P}almitoylation of
                      {T}heir {A}ccessory {S}ubunit {B}arttin to {B}e
                      {F}unctional.},
      journal      = {The journal of biological chemistry},
      volume       = {290},
      number       = {28},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2015-05015},
      pages        = {17390 - 17400},
      year         = {2015},
      abstract     = {CLC-K/barttin chloride channels are essential for NaCl
                      re-absorption in Henle's loop and for potassium secretion by
                      the stria vascularis in the inner ear. Here, we studied the
                      posttranslational modification of such channels by
                      palmitoylation of their accessory subunit barttin. We found
                      that barttin is palmitoylated in vivo and in vitro and
                      identified two conserved cysteine residues at positions 54
                      and 56 as palmitoylation sites. Point mutations at these two
                      residues reduce the macroscopic current amplitudes in cells
                      expressing CLC-K/barttin channels proportionally to the
                      relative reduction in palmitoylated barttin. CLC-K/barttin
                      expression, plasma membrane insertion, and single channel
                      properties remain unaffected, indicating that these
                      mutations decrease the number of active channels. R8W and
                      G47R, two naturally occurring barttin mutations identified
                      in patients with Bartter syndrome type IV, reduce barttin
                      palmitoylation and CLC-K/barttin channel activity.
                      Palmitoylation of the accessory subunit barttin might thus
                      play a role in chloride channel dysfunction in certain
                      variants of Bartter syndrome. We did not observe pronounced
                      alteration of barttin palmitoylation upon increased salt and
                      water intake or water deprivation, indicating that this
                      posttranslational modification does not contribute to long
                      term adaptation to variable water intake. Our results
                      identify barttin palmitoylation as a novel posttranslational
                      modification of CLC-K/barttin chloride channels.},
      cin          = {ICS-4},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-4-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:26013830},
      pmc          = {pmc:PMC4498076},
      UT           = {WOS:000357730900033},
      doi          = {10.1074/jbc.M114.631705},
      url          = {https://juser.fz-juelich.de/record/202863},
}