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Abstract
The need for disease-modifying drugs for Alzheimer’s disease has become increasingly important owing to escalating disease prevalence and the associated socio-economic burden. Until recently, reducing brain amyloid accumulation has been the main therapeutic focus; however, increasing evidence suggests that targeting abnormal tau phosphorylation could be beneficial. Tau is phosphorylated by several protein kinases and this is balanced by dephosphorylation by protein phosphatases. Phosphorylation at specific sites can influence the physiological functions of tau, including its role in binding to and stabilizing the neuronal cytoskeleton. aberrant phosphorylation of tau could render it susceptible to potentially pathogenic alterations, including conformational changes, proteolytic cleavage and aggregation. While strategies that reduce tau phosphorylation in transgenic models of disease have been promising, our understanding of the mechanisms through which tau becomes abnormally phosphorylated in disease is lacking.
Financial & competing interests disclosure
Diane P Hanger is in receipt of a grant held jointly with, and part-funded by GlaxoSmithKline. Work in the authors’ laboratories is funded by the Medical Research Council, the Wellcome Trust, the Alzheimer’s Society, the Alzheimer’s Research Trust and the Henry Smith Charity. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.
No writing assistance was utilized in the production of this manuscript.