% 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{Kang:30216,
      author       = {Kang, K. and Bauer, P. J. and Kinjo, T. G. and Szerencsei,
                      R. T. and Bönigk, W. and Winkfein, R. J. and Schnetkamp, P.
                      P. M.},
      title        = {{A}ssembly of retinal rod or cone
                      {N}a+/{C}a2+/{K}+-exchanger oligomers with c{GMP}-gated
                      channel subunits as probed with heterologously expressed
                      c{DNA}s},
      journal      = {Biochemistry},
      volume       = {42},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-30216},
      pages        = {4593 - 4600},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Proper control of intracellular free Ca(2+) is thought to
                      involve subsets of proteins that co-localize to mediate
                      coordinated Ca(2+) entry and Ca(2+) extrusion. The outer
                      segments of vertebrate rod and cone photoreceptors present
                      one example: Ca(2+) influx is exclusively mediated via
                      cGMP-gated channels (CNG), whereas the Na(+)/Ca(2+)-K(+)
                      exchanger (NCKX) is the only Ca(2+) extrusion protein
                      present. In situ, a rod NCKX homodimer and a CNG
                      heterotetramer are thought to be part of a single protein
                      complex. However, NCKX-NCKX and NCKX-CNG interactions have
                      been described so far only in bovine rod outer segment
                      membranes. We have used thiol-specific cross-linking and
                      co-immunoprecipitation to examine NCKX self-assembly and
                      CNG-NCKX co-assembly after heterologous expression of either
                      the rod or cone NCKX/CNG isoforms. Co-immunoprecipitation
                      clearly demonstrated both NCKX homooligomerization and
                      interactions between NCKX and CNG. The NCKX-NCKX and
                      NCKX-CNG interactions were observed for both the rod and the
                      cone isoforms. Thiol-specific cross-linking led to rod NCKX1
                      dimers and to cone NCKX2 adducts of an apparent molecular
                      weight higher than that predicted for a NCKX2 dimer. The
                      mass of the cross-link product critically depended on the
                      location of the particular cysteine residue used by the
                      cross-linker, and we cannot exclude that NCKX forms a higher
                      oligomer. The NCKX-NCKX and NCKX-CNG interactions were not
                      isoform-specific (i.e., rod NCKX could interact with cone
                      NCKX, rod NCKX could interact with cone CNGA, and vice
                      versa). Deletion of the two large hydrophilic loops from the
                      NCKX protein did not abolish the NCKX oligomerization,
                      suggesting that it is mediated by the highly conserved
                      transmembrane spanning segments.},
      keywords     = {Animals / Calcium: metabolism / Cell Line / Chickens:
                      metabolism / Cyclic GMP: metabolism / Cyclic
                      Nucleotide-Gated Cation Channels / Humans / Insects / Ion
                      Channels: metabolism / Photoreceptor Cells, Vertebrate:
                      metabolism / Precipitin Tests / Sodium-Calcium Exchanger:
                      biosynthesis / Sodium-Calcium Exchanger: metabolism / Cyclic
                      Nucleotide-Gated Cation Channels (NLM Chemicals) / Ion
                      Channels (NLM Chemicals) / Sodium-Calcium Exchanger (NLM
                      Chemicals) / potassium-dependent sodium-calcium exchanger
                      (NLM Chemicals) / Calcium (NLM Chemicals) / Cyclic GMP (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB57},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:12693957},
      UT           = {WOS:000182420000031},
      doi          = {10.1021/bi027276z},
      url          = {https://juser.fz-juelich.de/record/30216},
}