Tau protein isoforms, phosphorylation and role in neurodegenerative disorders

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3

This review attempts to summarize what is known about tau phosphorylation in the context of both normal cellular function and dysfunction. However, conceptions of tau function continue to evolve, and it is likely that the regulation of tau distribution and metabolism is complex. The roles of microtubule-associated kinases and phosphatases have yet to be fully described, but may afford insight into how tau phosphorylation at the distal end of the axon regulates cytoskeletal-membrane interactions. Finally, lipid and glycosaminoglycan modification of tau structure affords yet more complexity for regulation and aggregation. Continued work will help to determine what is causal and what is coincidental in Alzheimer's disease, and may lead to identification of therapeutic targets for halting the progression of paired helical filament formation.

Regulated phosphorylation and dephosphorylation of tau protein : effects on microtubule interaction, intracellular trafficking and neurodegeneration

Phosphorylation of Microtubule-associated Protein Tau Is Regulated by Protein Phosphatase 2A in Mammalian Brain IMPLICATIONS FOR NEUROFIBRILLARY DEGENERATION IN ALZHEIMER'S DISEASE

J. Henley

Papers

The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.