% 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{Guzman:838399,
      author       = {Guzman, Raul and Franzen, Arne and Bungert, Stefanie and
                      Fahlke, Christoph},
      title        = {{P}referential {A}ssociation with {C}l{C}-3 {P}ermits
                      {S}orting of {C}l{C}-4 into {E}ndosomal {C}ompartments},
      journal      = {The journal of biological chemistry},
      volume       = {292},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2017-07011},
      pages        = {19055-19065},
      year         = {2017},
      abstract     = {ClC-4 is an intracellular Cl--H+ exchanger, which is highly
                      expressed in the brain and whose dysfunction has been linked
                      to intellectual disability and epilepsy. We here studied the
                      subcellular localization of human ClC-4 in heterologous
                      expression systems. ClC-4 is retained in the endoplasmic
                      reticulum (ER) upon overexpression in HEK293T cells.
                      Co-expression with distinct ClC-3 splice variants targets
                      ClC-4 to late endosome/lysosomes (ClC-3a and ClC-3b),
                      recycling endosome (ClC-3c) or to the Golgi (ClC-3e). When
                      expressed in cultured astroctyes ClC-4 sorts to endocytic
                      compartments in WT cells, but was retained in the ER in
                      Clcn3-/- cells. To understand the virtual absence of ER
                      localized ClC-4 in WT cells we performed association studies
                      by high resolution clear native gel electrophoresis (hrCNE).
                      Whereas other CLCm channels and transporters form stable
                      dimers, ClC-4 was mostly observed as monomer, with
                      ClC-3-ClC-4 heterodimers being more stable than ClC-4
                      homodimers. We conclude that unique oligomerization
                      properties of ClC-4 permits regulated targeting of ClC-4 to
                      various endosomal compartments system via expression of
                      different ClC-3 splice variants.},
      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:28972156},
      UT           = {WOS:000415848000028},
      doi          = {10.1074/jbc.M117.801951},
      url          = {https://juser.fz-juelich.de/record/838399},
}