Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 290, Issue 11, Pages 7087-7096Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M114.614750
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Funding
- ministry of science, ICT, and future planning ((MSIP) [NRF-2012R1A2A2A01012923, NRF-2012R1A4A1028200, NRF-2013R1A1A2074251]
- national research foundation (NRF) of Korea [NRF-2012K2A1A2033117]
- POSTECH basic science research institute (BSRI) Fund
- Grants-in-Aid for Scientific Research [25670488, 15K15399, 24390271] Funding Source: KAKEN
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Dysbindin and DISC1 are schizophrenia susceptibility factors playing roles in neuronal development. Here we show that the physical interaction between dysbindin and DISCI is critical for the stability of dysbindin and for the process of neurite outgrowth. We found that DISCI forms a complex with dysbindin and increases its stability in association with a reduction in ubiquitylation. Furthermore, knockdown of DISCI or expression of a deletion mutant, DISCI lacking amino acid residues 403-504 of DISC1 (DISC1(Delta 403-504)), effectively decreased levels of endogenous dysbindin. Finally, the neurite outgrowth defect induced by knockdown of DISCI was partially reversed by coexpression of dysbindin. Taken together, these results indicate that dysbindin and DISC1 form a physiologically functional complex that is essential for normal neurite outgrowth.
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