It is noteworthy that many of the alcohol-sensitive proteins that were significantly changed in our proteomic networks are also associated with major neurodegenerative diseases such as AD and schizophrenia (Hensley, Venkova, Christov, Gunning, & Park, 2011; Martins-De-Souza et al., 2010). The DPYSL protein, which was significantly downregulated in the amygdala network, stands out for many reasons and may be an ideal therapeutic target for AD. The gene DPYSL encodes a protein called collapsin response mediator protein 2 (CRMP2) which is a member of a family of CRMP proteins that regulate microtubule formation and axonal growth (Charrier et al., 2003). CRMP is highly expressed in the CNS and it is important for microtubule formation and stability, vesicle trafficking and ion channel stability, among other functions. There has been exponential interest in the functional role of this protein in disease pathology because it is hyperphosphorylated in the brains of both AD patients and it is known to be a key phosphorylation substrate for GSK3β, CDK5 and CAMKII (Soutar, Thornhill, Cole, & Sutherland, 2009). Phosphorylation of CRMP at these sites renders it unable
