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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Yoshida, H. et al.

Yoshida, Hastie, McLauchlan, Cohen, Goedert,

Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase ( JNK).

Microtubule-associated protein tau in a hyperphosphorylated state is the major component of the filamentous lesions that define a number of neurodegenerative diseases commonly referred to as tauopathies. Hyperphosphorylation of tau at most sites appears to precede filament assembly. Many of the hyperphosphorylated sites are serine/threonine-proline sequences. Here we show that c-Jun N-terminal kinases JNK1, JNK2 and JNK3 phosphorylate tau at many serine/threonine-prolines, as assessed by the generation of the epitopes of phosphorylation-dependent anti-tau antibodies. Of the three protein kinases, JNK2 phosphorylated the most sites in tau, followed by JNK3 and JNK1. Phosphorylation by JNK isoforms resulted in a greatly reduced ability of tau to promote microtubule assembly. These findings extend the number of candidate protein kinases for the hyperphosphorylation of tau in Alzheimer's disease and other neurodegenerative disorders.[1]

References

Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase (JNK). Yoshida, H., Hastie, C.J., McLauchlan, H., Cohen, P., Goedert, M. J. Neurochem. (2004) [Pubmed]

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