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 to function properly and is proximally associated with plaque and tangle formations in AD brains (Yoshida, Watanabe, & Ihara, 1998). Further, it has been shown that CRMP2 co-aggregates with Tau in 3xTg mice at an early age, suggesting that CRMP could be used as an early biomarker for AD, prior to expression of significant behavioral deficits (Cole et al., 2007).
