REGULATED PHOSPHORYLATION AND DEPHOSPHORYLATION OF TAU-PROTEIN - EFFECTS ON MICROTUBULE INTERACTION, INTRACELLULAR TRAFFICKING AND NEURODEGENERATION

This review attempts to summarize what is known about tau phosphorylat ion in the context of both normal cellular function and dysfunction. H owever, conceptions of tau function continue to evolve, and it is like ly that the regulation of tau distribution and metabolism is complex. The roles of micro tubule-associated kinases and phosphatases have yet to be fully described, but may afford insight into how tau phosphoryl ation at the distal end of the axon regulates cytoskeletal-membrane in teractions. Finally, lipid and glycosaminoglycan modification of tau s tructure affords yet more complexity for regulation and aggregation. C ontinued work will help to determine what is causal and what is coinci dental in Alzheimer's disease, and may lead to identification of thera peutic targets for halting the progression of paired helical filament formation.