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@ARTICLE{Hwang:41869,
      author       = {Hwang, J.-Y. and Schlesinger, R. and Koch, K.-W.},
      title        = {{I}rregular dimerization of guanylate cyclase-activating
                      protein 1 mutants causes loss of target activation},
      journal      = {The FEBS journal},
      volume       = {271},
      issn         = {0014-2956},
      address      = {Oxford [u.a.]},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-41869},
      pages        = {3785 - 3793},
      year         = {2004},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Guanylate cyclase-activating proteins (GCAPs) are neuronal
                      calcium sensors that activate membrane bound guanylate
                      cyclases (EC 4.6.1.2.) of vertebrate photoreceptor cells
                      when cytoplasmic Ca2+ decreases during illumination. GCAPs
                      contain four EF-hand Ca2+-binding motifs, but the first
                      EF-hand is nonfunctional. It was concluded that for GCAP-2,
                      the loss of Ca2+-binding ability of EF-hand 1 resulted in a
                      region that is crucial for targeting guanylate cyclase
                      [Ermilov, A.N., Olshevskaya, E.V. $\&$ Dizhoor, A.M. (2001)
                      J. Biol. Chem.276, 48143-48148]. In this study we tested the
                      consequences of mutations in EF-hand 1 of GCAP-1 with
                      respect to Ca2+ binding, Ca2+-induced conformational changes
                      and target activation. When the nonfunctional first EF-hand
                      in GCAP-1 is replaced by a functional EF-hand the chimeric
                      mutant CaM-GCAP-1 bound four Ca2+ and showed similar
                      Ca2+-dependent changes in tryptophan fluorescence as the
                      wild-type. CaM-GCAP-1 neither activated nor interacted with
                      guanylate cyclase. Size exclusion chromatography revealed
                      that the mutant tended to form inactive dimers instead of
                      active monomers like the wild-type. Critical amino acids in
                      EF-hand 1 of GCAP-1 are cysteine at position 29 and proline
                      at position 30, as changing these to glycine was sufficient
                      to cause loss of target activation without a loss of
                      Ca2+-induced conformational changes. The latter mutation
                      also promoted dimerization of the protein. Our results show
                      that EF-hand 1 in wild-type GCAP-1 is critical for providing
                      the correct conformation for target activation.},
      keywords     = {Amino Acid Sequence / Animals / Calcium: metabolism /
                      Calcium-Binding Proteins: chemistry / Calcium-Binding
                      Proteins: genetics / Calcium-Binding Proteins: isolation
                      $\&$ purification / Calcium-Binding Proteins: metabolism /
                      Chromatography, Gel / Cysteine: metabolism / Dimerization /
                      EF Hand Motifs: genetics / Escherichia coli: genetics /
                      Guanylate Cyclase-Activating Proteins / Light Signal
                      Transduction / Molecular Sequence Data / Mutation / Proline:
                      metabolism / Protein Conformation / Reactive Oxygen Species:
                      metabolism / Recombinant Proteins: chemistry / Recombinant
                      Proteins: metabolism / Sequence Homology, Amino Acid /
                      Spectrometry, Fluorescence / Calcium-Binding Proteins (NLM
                      Chemicals) / Guanylate Cyclase-Activating Proteins (NLM
                      Chemicals) / Reactive Oxygen Species (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / Proline (NLM
                      Chemicals) / Cysteine (NLM Chemicals) / Calcium (NLM
                      Chemicals) / J (WoSType)},
      cin          = {IBI-1 / IBI-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB57 / I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:15355355},
      UT           = {WOS:000223711400017},
      doi          = {10.1111/j.1432-1033.2004.04320.x},
      url          = {https://juser.fz-juelich.de/record/41869},
}