Open Access
The role of tau phosphorylation and cleavage in neuronal cell death
Wanjoo Chun1,Gail V W Johnson1
Department of Psychiatry, School of Medicine, University of Alabama at Birmingham, 1061 Sparks Center, 1720 7th Avenue South, Birmingham, AL 35294-0017, USA
DOI: 10.2741/2097 Volume 12 Issue 2, pp.733-756
Published: 01 January 2007
(This article belongs to the Special Issue Mechanisms of neuronal Injury in neurological diseases)

The microtubule-associated protein tau is the primary component of the intracellular filamentous deposits found in Alzheimer's disease (AD) brain and also in a family of neurodegenerative diseases called 'tauopathies', where tau pathology is the primary, defining characteristic with little or no amyloid-beta (Abeta) pathology. It has been demonstrated that tau modifications such as hyperphosphorylation and truncation might be important events in the process leading to tau intracellular aggregation and neuronal cell death. The discovery of tau gene mutations in frontotemporal dementia with parkinsonism linked to chromosome 17 (FTDP-17) reinforced the predominant role attributed to tau proteins in the pathogenesis of neurodegenerative disorders. This review highlights recent findings concerning the normal metabolism and function of tau, as well as the abnormal processing and function of tau in AD and in the tauopathies.

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Wanjoo Chun, Gail V W Johnson. The role of tau phosphorylation and cleavage in neuronal cell death. Frontiers in Bioscience-Landmark. 2007. 12(2); 733-756.