Format

Send to

Choose Destination
Neuron. 1993 Jul;11(1):153-63.

Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding.

Author information

1
Max-Planck-Unit for Structural Molecular Biology DESY, Hamburg Federal Republic of Germany.

Abstract

Tau protein, a component of Alzheimer paired helical filaments, can be phosphorylated by several kinases. Of particular interest is the phosphorylation at Ser/Thr-Pro motifs because the resulting state of tau is similar to that found in Alzheimer's disease, as judged by its immunoreactivity. This state can be mimicked by a brain extract kinase activity and by MAP kinase. We have now studied the effect of these modes of phosphorylation on the interaction between tau and microtubules. Although MAP kinase efficiently phosphorylates many Ser/Thr-Pro motifs of tau, its effect on microtubule binding is only moderate. By contrast, phosphorylation of a single residue, Ser262, has a major effect on binding. Ser262 is not phosphorylated by MAP kinase or other proline-directed kinases, but is phosphorylated by a 35/41 kd kinase in brain, whose purification is described.

PMID:
8393323
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center