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Cytosolic protein interactions of the schizophrenia susceptibility gene dysbindin
Author(s) -
Mead CarriLyn R.,
Kuzyk Michael A.,
Moradian Annie,
Wilson Gary M.,
Holt Robert A.,
Morin Gregg B.
Publication year - 2010
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2010.06690.x
Subject(s) - immunoprecipitation , microbiology and biotechnology , biology , signal transducing adaptor protein , exocyst , biogenesis , protein–protein interaction , cytosol , vacuolar protein sorting , gene , endosome , genetics , biochemistry , signal transduction , protein subunit , enzyme , intracellular
J. Neurochem. (2010) 113 , 1491–1503. Abstract Using immunoprecipitation, mass spectrometry, and western blot analysis we investigated cytosolic protein interactions of the schizophrenia susceptibility gene dysbindin in mammalian cells. We identified novel interactions with members of the exocyst, dynactin and chaperonin containing T‐complex protein complexes, and we confirmed interactions reported previously with all members of the biogenesis of lysosome‐related organelles complex‐1 and the adaptor‐related protein complex 3. We report interactions between dysbindin and the exocyst and dynactin complex that confirm a link between two important schizophrenia susceptibility genes: dysbindin and disrupted‐in‐schizophrenia‐1. To expand upon this network of interacting proteins we also investigated protein interactions for members of the exocyst and dynactin complexes in mammalian cells. Our results are consistent with the notion that impairment of aspects of the synaptic vesicle life cycle may be a pathogenic mechanism in schizophrenia.