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| Hauptseite > Publikationsdatenbank > Oligomer assembly of the C-terminal DISC1 domain (640-854) is controlled by self-association motifs and disease-associated polymorphism S704C > print |
| Hauptseite > Publikationsdatenbank > Oligomer assembly of the C-terminal DISC1 domain (640-854) is controlled by self-association motifs and disease-associated polymorphism S704C > print |
| 001 | 6507 | ||
| 005 | 20200402205709.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:19583211 |
| 024 | 7 | _ | |2 DOI |a 10.1021/bi900901e |
| 024 | 7 | _ | |2 WOS |a WOS:000268720300021 |
| 024 | 7 | _ | |a altmetric:3455235 |2 altmetric |
| 037 | _ | _ | |a PreJuSER-6507 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 570 |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 100 | 1 | _ | |0 P:(DE-Juel1)VDB72260 |a Leliveld, S. R. |b 0 |u FZJ |
| 245 | _ | _ | |a Oligomer assembly of the C-terminal DISC1 domain (640-854) is controlled by self-association motifs and disease-associated polymorphism S704C |
| 260 | _ | _ | |a Columbus, Ohio |b American Chemical Society |c 2009 |
| 300 | _ | _ | |a 7746 - 7755 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 798 |a Biochemistry |v 48 |x 0006-2960 |y 32 |
| 500 | _ | _ | |a 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. |
| 520 | _ | _ | |a 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. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK409 |2 G:(DE-HGF) |a Funktion und Dysfunktion des Nervensystems |c P33 |x 0 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a Animals |
| 650 | _ | 2 | |2 MeSH |a Antibodies, Monoclonal: metabolism |
| 650 | _ | 2 | |2 MeSH |a Humans |
| 650 | _ | 2 | |2 MeSH |a Mice |
| 650 | _ | 2 | |2 MeSH |a Nerve Tissue Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Nerve Tissue Proteins: genetics |
| 650 | _ | 2 | |2 MeSH |a Nerve Tissue Proteins: metabolism |
| 650 | _ | 2 | |2 MeSH |a Polymorphism, Genetic |
| 650 | _ | 2 | |2 MeSH |a Protein Multimerization |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Quaternary |
| 650 | _ | 2 | |2 MeSH |a Protein Structure, Tertiary |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Antibodies, Monoclonal |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a DISC1 protein, human |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Nerve Tissue Proteins |
| 650 | _ | 7 | |2 WoSType |a J |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Hendriks, P. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Michel, M. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Sajnani, G. |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Bader, V. |b 4 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Trossbach, S. |b 5 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Prikulis, I. |b 6 |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB57647 |a Hartmann, R. |b 7 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB20019 |a Jonas, E. |b 8 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, D. |b 9 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Requena, J. R. |b 10 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Korth, C. |b 11 |
| 773 | _ | _ | |0 PERI:(DE-600)1472258-6 |a 10.1021/bi900901e |g Vol. 48, p. 7746 - 7755 |p 7746 - 7755 |q 48<7746 - 7755 |t Biochemistry |v 48 |x 0006-2960 |y 2009 |
| 856 | 7 | _ | |u http://dx.doi.org/10.1021/bi900901e |
| 909 | C | O | |o oai:juser.fz-juelich.de:6507 |p VDB |
| 913 | 1 | _ | |0 G:(DE-Juel1)FUEK409 |a DE-HGF |b Gesundheit |k P33 |l Funktion und Dysfunktion des Nervensystems |v Funktion und Dysfunktion des Nervensystems |x 0 |
| 914 | 1 | _ | |y 2010 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)VDB942 |d 31.12.2010 |g ISB |k ISB-3 |l Strukturbiochemie |x 0 |
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| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
| 981 | _ | _ | |a I:(DE-Juel1)ICS-6-20110106 |
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