Tau phosphorylation in neuronal cell function and dysfunction.

Abstract:

:Tau is a group of neuronal microtubule-associated proteins that are formed by alternative mRNA splicing and accumulate in neurofibrillary tangles in Alzheimer's disease (AD) brain. Tau plays a key role in regulating microtubule dynamics, axonal transport and neurite outgrowth, and all these functions of tau are modulated by site-specific phosphorylation. There is significant evidence that a disruption of normal phosphorylation events results in tau dysfunction in neurodegenerative diseases, such as AD, and is a contributing factor to the pathogenic processes. Indeed, the abnormal tau phosphorylation that occurs in neurodegenerative conditions not only results in a toxic loss of function (e.g. decreased microtubule binding) but probably also a toxic gain of function (e.g. increased tau-tau interactions). Although tau is phosphorylated in vitro by numerous protein kinases, how many of these actually phosphorylate tau in vivo is unclear. Identification of the protein kinases that phosphorylate tau in vivo in both physiological and pathological processes could provide potential therapeutic targets for the treatment of AD and other neurodegenerative diseases in which there is tau pathology.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Johnson GV,Stoothoff WH

doi

10.1242/jcs.01558

keywords:

subject

Has Abstract

pub_date

2004-11-15 00:00:00

pages

5721-9

issue

Pt 24

eissn

0021-9533

issn

1477-9137

pii

117/24/5721

journal_volume

117

pub_type

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