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p^44^^mpk^ MAP kinase induces aizheimer type alterations in tau function and in primary hippocampal neurons by Q. Lu; J. P. Soria; J. G. Wood is a Neuroscience article available to read on EtoBox.

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Abnormally phosphorylated tau protein is a major component of the cytoskeletal pathology of Alzheimer's disease (AD) found in the neurofibrillary tangle (NFT) and neuritic plaque (NP). Identification of the kinase responsible for this phosphorylation has been difficult. In the test tube, several proline-directed kinases, particularly mitogen-activated protein (MAP) and cdc2 kinase, phosphorylate tau on sites that appear to mimic the abnormally phosphorylated sites in AD. Important unanswered issues include: 1) whether this phosphorylation event occurs in the tightly regulated environment of a living cell; 2) whether this phosphorylation of tau affects its functional properties; and 3) what is the subcellular relationship of proline-directed kinases and tau. We show here that tau can be phosphorylated in cultured hippocampal neurons by the MAP kinase pampk, and phosphorylation of tau compromises its functional ability to assemble microtubules. We show further that MAP kinase copurifies with microtubule fractions where it is tyrosine phosphorylated and presumably active. These studies address and raise several important issues regarding the regulation of tau phosphorylation in normal

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Author

Q. Lu; J. P. Soria; J. G. Wood

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0360-4012)

Published

1993

Language

EN

Field

Neuroscience (Life Sciences)