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Article Addendum

The interaction of schizophrenia-related proteins DISC1 and NDEL1, in light of the newly identified domain structure of DISC1

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Article: e1335375 | Received 11 May 2017, Accepted 22 May 2017, Published online: 06 Jul 2017

References

  • Yerabham ASK, Weiergräber OH, Bradshaw NJ, Korth C. Revisiting Disrupted-in-Schizophrenia 1 as a scaffold protein. Biol Chem 2013; 394(11):1425-37; PMID:23832957; https://doi.org/10.1515/hsz-2013-0178
  • Bradshaw NJ, Hayashi MAF. NDE1 and NDEL1 from genes to (mal)functions: parallel but distinct roles impacting on neurodevelopmental disorders and psychiatric illness. Cell Mol Life Sci 2017; 74(7):1191-210; PMID:27742926; https://doi.org/10.1007/s00018-016-2395-7
  • Brandon NJ, Handford EJ, Schurov I, Rain J-C, Pelling M, Duran-Jimeniz B, Camargo LM, Oliver KR, Beher D, Shearman MS, Whiting PJ. Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally regulated complex: implications for schizophrenia and other major neurological disorders. Mol Cell Neurosci 2004; 25(1):42-55; PMID:14962739; https://doi.org/10.1016/j.mcn.2003.09.009
  • Bradshaw NJ, Hennah W, Soares DC. NDE1 and NDEL1: twin neurodevelopmental proteins with similar ‘nature’ but different ‘nurture’. Biomol Concepts 2013; 4(5):447-64; PMID:24093049; https://doi.org/10.1515/bmc-2013-0023
  • Morris JA, Kandpal G, Ma L, Austin CP. DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Hum Mol Genet 2003; 12(13):1591-608; PMID:12812986; https://doi.org/10.1093/hmg/ddg162
  • Kamiya A, Tomoda T, Chang J, Takaki M, Zhan C, Morita M, Cascio MB, Elashvili S, Koizumi H, Takanezawa Y, et al. DISC1-NDEL1/NUDEL protein interaction, an essential component for neurite outgrowth, is modulated by genetic variations of DISC1. Hum Mol Genet 2006; 15(22):3313-23; PMID:17035248; https://doi.org/10.1093/hmg/ddl407
  • Yerabham ASK, Mas PJ, Decker C, Soares DC, Weiergräber OH, Nagel-Steger L, Willbold D, Hart DJ, Bradshaw NJ, Korth C. A structural organization for the Disrupted in Schizophrenia 1 protein, identified by high-throughput screening, reveals distinctly folded regions, which are bisected by mental illness-related mutations. J Biol Chem 2017; 292(16):6468-77; PMID:28249940; https://doi.org/10.1074/jbc.M116.773903
  • Mas PJ, Hart DJ. ESPRIT: a method for defining soluble expression constructs in poorly understood gene sequences. In: Burgess-Brown NA, editor. Heterologous gene expression in E.coli: methods and protocols. New York: Human Press; 2017. 45-63; PMID:28470598; https://doi.org/10.1007/978-1-4939-6887-9_4
  • Buchan DWA, Minneci F, Nugent TCO, Bryson K, Jones DT. Scalable web services for the PSIPRED Protein Analysis Workbench. Nucleic Acids Res 2013; 41(Web Server Issue):W349-57; PMID:23748958; https://doi.org/10.1093/nar/gkt381
  • Narayanan S, Arthanari H, Wolfe MS, Wagner G. Molecular characterization of Disrupted in Schizophrenia-1 risk variant S704C reveals the formation of altered oligomeric assembly. J Biol Chem 2011; 286(51):44266-76; PMID:21998303; https://doi.org/10.1074/jbc.M111.271593
  • Leliveld SR, Bader V, Hendricks P, Prikulis I, Sajnani G, Requena JR, Korth C. Insolubility of disrupted-in-schizophrenia 1 disrupts oligomer-dependent interactions with nuclear distribution element 1 and is associated with sporadic mental disease. J Neurosci 2008; 28(15):3839-45; PMID:18400883; https://doi.org/10.1523/JNEUROSCI.5389-07.2008
  • Leliveld SR, Hendricks P, Michel M, Sajnani G, Bader V, Trossbach S, Prikulis I, Hartmann R, Jonas E, Willbold D, et al. Oligomer assembly of the C-terminal DISC1 domain (640-854) is controlled by self-association motifs and disease-associated polymorphism S704C. Biochemistry 2009; 48(32):7746-55; PMID:19583211; https://doi.org/10.1021/bi900901e
  • Soares DC, Bradshaw NJ, Zou J, Kennaway CK, Hamilton RS, Chen ZA, Wear MA, Blackburn EA, Braham J, Böttcher B, et al. The mitosis and neurodevelopmental proteins NDE1 and NDEL1 form dimers, tetramers, and polymers with a folded back structure in solution. J Biol Chem 2012; 287(39):32381-93; PMID:22843697; https://doi.org/10.1074/jbc.M112.393439
  • Hayashi MAF, Portaro FCV, Bastos MF, Guerreiro JR, Oliveira V, Gorrão SS, Tambourgi DV, Sant'Anna OA, Whiting PJ, Camargo LM, et al. Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase activity by disrupted-in-schizophrenia 1. Proc Natl Acad Sci U S A 2005; 102(10):3828-33; PMID:15728732; https://doi.org/10.1073/pnas.0500330102
  • Tarricone C, Perrina F, Monzani S, Massimiliano L, Kim M-H, Derewenda ZS, Knapp S, Tsai L-H, Musacchio A. Coupling PAF signaling to dynein regulation: structure of LIS1 in complex with PAF-acetylhydrolase. Neuron 2004; 44(5):809-21; PMID:15572112
  • McKenney RJ, Weil SJ, Scherer J, Vallee RB. Mutually exclusive cytoplasmic dynein regulation by NudE-Lis1 and dynactin. J Biol Chem 2011; 286(45):39615-22; PMID:21911489; https://doi.org/10.1074/jbc.M111.289017
  • Burdick KE, Kamiya A, Hodgkinson CA, Lencz T, DeRosse P, Ishizuka K, Elashvili S, Arai H, Goldman D, Sawa A, Malhorta AK. Elucidating the relationship between DISC1, NDEL1 and NDE1 and the risk for schizophrenia: evidence of epistasis and competitive binding. Hum Mol Genet 2008; 17(16):2462-73; PMID:18469341; https://doi.org/10.1093/hmg/ddn146