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Description
Disrupted-In-Schizophrenia 1 (DISC1) is associated with schizophrenia by multiple genetic studies. DISC1 might cause susceptibility to schizophrenia. DISC1 has distinct interaction domains: MAP1A interacts via its LC2 domain with the N-terminus of DISC1, whereas MIPT3 and NUDEL bind via their C-terminal domains to the central coiled-coil domain of DISC1, and ATF4/5 bind via their C-terminal domains to the C-terminus of DISC1. DISC1 protein localizes to predominantly perinuclear punctate structures which extend into neurites in some cells. DISC1 is a multifunctional protein whose truncation contributes to schizophrenia susceptibility by disrupting intracellular transport, neurite architecture and/or neuronal migration, all of which have been hypothesized to be pathogenic in the schizophrenic brain. DISC1 interacts with Nudel through a leucine zipper domain and binds to a novel DISC1-interaction domain on Nudel, which is independent from the Lis1 binding site. Nudel is able to act as a bridge between DISC1 and Lis1 to allow formation of a trimolecular complex. Nudel has been implicated to play a role in neuronal migration, together with the developmental variation in the abundance of the DISC1-Nudel complex, may implicate a defective DISC1-Nudel complex as a neurodevelopmental cause of schizophrenia.
Immunogen
Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human DISC1 (Disrupted in schizophrenia 1 protein)