Phosphorylation of tau by proline-directed protein kinase (p34cdc2/p58cyclin A) decreases tau-induced microtubule assembly and antibody SMI33 reactivity
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Tau pathophysiology in neurodegeneration: a tangled issue
2009, Trends in NeurosciencesCitation Excerpt :With tau containing >80 possible phosphorylation sites in its primary amino acid structure, nearly 20% of the molecule can be phosphorylated and a large number of protein kinases (>20) and phosphatases have been identified that control tau phosphorylation [66]. Some of the most widely studied kinases and phosphatases that have been implicated in the pathological phosphorylation of tau are glycogen synthase kinase 3β (GSK3β) [67,68], microtubule affinity regulating kinase (MARK) [69], mitogen activated protein kinase [70] and cyclin dependent kinase 5 (Cdk5) [71–75], with protein phosphatase 2A being the most important tau phosphatase [76–78]. With so many phosphorylation sites and kinases and phosphatases regulating the phosphorylation state of tau, it is clear that the phosphorylation state of tau is very highly regulated and important in its normal and pathological function.
Interaction of tau with the neural membrane cortex is regulated by phosphorylation at sites that are modified in paired helical filaments
2000, Journal of Biological ChemistryThe microtubule binding of tau and high molecular weight tau in apoptotic PC12 cells is impaired because of altered phosphorylation
1999, Journal of Biological ChemistryDifferential cytoskeletal changes during growth cone collapse in response to hSema III and thrombin
1999, Molecular and Cellular Neurosciences