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@ARTICLE{Leliveld:6507,
      author       = {Leliveld, S. R. and Hendriks, P. and Michel, M. and
                      Sajnani, G. and Bader, V. and Trossbach, S. and Prikulis, I.
                      and Hartmann, R. and Jonas, E. and Willbold, D. and Requena,
                      J. R. and Korth, C.},
      title        = {{O}ligomer assembly of the {C}-terminal {DISC}1 domain
                      (640-854) is controlled by self-association motifs and
                      disease-associated polymorphism {S}704{C}},
      journal      = {Biochemistry},
      volume       = {48},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-6507},
      pages        = {7746 - 7755},
      year         = {2009},
      note         = {Funded by a research grant (LE 2197/1-1) to S.R.L. from the
                      German Research Foundation (DFG) and Stanley Medical
                      Research Institute, Baltimore, MD, to C.K.},
      abstract     = {Genetic studies have established a role of
                      disrupted-in-schizophrenia-1 (DISC1) in chronic mental
                      diseases (CMD). Limited experimental data are available on
                      the domain structure of the DISC1 protein although multiple
                      interaction partners are known including a self-association
                      domain within the middle part of DISC1 (residues 403-504).
                      The DISC1 C-terminal domain is deleted in the original
                      Scottish pedigree where DISC1 harbors two coiled-coil
                      domains and disease-associated polymorphisms at 607 and 704,
                      as well as the important nuclear distribution element-like 1
                      (NDEL1) binding site at residues 802-839. Here, we performed
                      mutagenesis studies of the C-terminal domain of the DISC1
                      protein (residues 640-854) and analyzed the expressed
                      constructs by biochemical and biophysical methods. We
                      identified novel DISC1 self-association motifs and the
                      necessity of their concerted action for orderly assembly:
                      the region 765-854 comprising a coiled-coil domain is a
                      dimerization domain and the region 668-747 an
                      oligomerization domain; dimerization was found to be a
                      prerequisite for orderly assembly of oligomers. Consistent
                      with this, disease-associated polymorphism C704 displayed a
                      slightly higher oligomerization propensity. The
                      heterogeneity of DISC1 multimers in vitro was confirmed with
                      a monoclonal antibody binding exclusively to HMW multimers.
                      We also identified C-terminal DISC1 fragments in human
                      brains, suggesting that C-terminal fragments could carry out
                      DISC1-dependent functions. When the DISC1 C-terminal domain
                      was transiently expressed in cells, it assembled into a
                      range of soluble and insoluble multimers with distinct
                      fractions selectively binding NDEL1, indicating
                      functionality. Our results suggest that assembly of the
                      C-terminal domain is controlled by distinct domains
                      including the disease-associated polymorphism 704 and is
                      functional in vivo.},
      keywords     = {Animals / Antibodies, Monoclonal: metabolism / Humans /
                      Mice / Nerve Tissue Proteins: chemistry / Nerve Tissue
                      Proteins: genetics / Nerve Tissue Proteins: metabolism /
                      Polymorphism, Genetic / Protein Multimerization / Protein
                      Structure, Quaternary / Protein Structure, Tertiary /
                      Antibodies, Monoclonal (NLM Chemicals) / DISC1 protein,
                      human (NLM Chemicals) / Nerve Tissue Proteins (NLM
                      Chemicals) / J (WoSType)},
      cin          = {ISB-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19583211},
      UT           = {WOS:000268720300021},
      doi          = {10.1021/bi900901e},
      url          = {https://juser.fz-juelich.de/record/6507},
}