Cyclin-dependent protein kinase 5 (Cdk5) is a unique member of the family of cyclin-dependent kinases that is not directly involved in the progression of proliferating cells through the cell cycle (1). Distributed in most tissues and various cell lines, Cdk5 is active primarily in neuronal tissues, because of its association with neuron-specific activators such as p35 (a neural-specific regulatory subunit of Cdk5) (2). In addition to its role in muscle and neuronal differentiation, Cdk5 also contributes to the assembly, organization and stability of the axonal cytoskeleton in neurons, promotes neurite outgrowth and axon guidance in developing neurons, participates in the regulation of synaptic transmission and provides an additional pathway to cellular apoptosis (3-5). Cdk5 phosphorylates MAP1b, Tau, neurofilament proteins, caldesmon and proteins of the synaptic vesicles. Deregulation of Cdk5 has profound cytotoxic effects and is implicated in the development of neurodegenerative diseases such as Alzheimer's disease and amyotrophic lateral sclerosis. Recent studies have showed that increased kinase activity of the p35/Cdk5 complex in developing neurons is observed when Cdk5 is phosphorylated at Y15 by c-Abl tyrosine kinase; this activity is further enhanced by Cable (6).
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Western blot analysis on A) Hela + AP treated B) Hela cell lyasate using Pan Cdk5 and C) Hela + AP treated D) Hela cell lysate using Phospho Cdk5 (pY15), dilution 1:2000.