Abstract
untransfected cells. Overexpression of cdk-5 induced a dramatic increase in phosphorylation of NFs and z at several phosphorylation sites. Examined by using time-lapse imaging of fluorescence of enhanced green fluorescence protein linked to N-terminus of NF-M (EGFP-NF-M) that was transiently transfected into the N2a cells, we found that the overactivation of cdk-5 also slowed down axonal transport of NF and induced immobile NF clusters and accumulation of mitochondria in the cell body. These results provide direct evidence that cdk-5-catalyzed hyperphosphorylation of cytoskeletaI proteins can induce axonal transport impairment of NFs and other organelles. Thus, a deregulation of cdk-5-catalyzed phosphorylation of these proteins might underlie the molecular mechanism of neurofibrillary degeneration of AD. #
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