p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]

M Goedert; E S Cohen; R Jakes; P Cohen

doi:10.1016/0014-5793(92)81418-l

p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]

FEBS Lett. 1992 Nov 2;312(1):95-9. doi: 10.1016/0014-5793(92)81418-l.

Authors

M Goedert¹, E S Cohen, R Jakes, P Cohen

Affiliation

¹ MRC Laboratory of Molecular Biology, Cambridge, UK.

PMID: 1330687
DOI: 10.1016/0014-5793(92)81418-l

Abstract

The paired helical filament (PHF), which comprises the major fibrous element of the neurofibrillary tangle of Alzheimer's disease, is composed of abnormally phosphorylated microtubule-associated protein tau. Here we show that p42 MAP kinase phosphorylates recombinant tau and converts it to a form which is similar to PHF tau. Of the major serine/threonine protein phosphatases found in mammalian tissues only protein phosphatase 2A (PP2A) could dephosphorylate tau phosphorylated in this manner, with PP2A1 being the most effective form of the enzyme.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Brain / metabolism
Calcium / pharmacology
Calcium-Calmodulin-Dependent Protein Kinases
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Ethers, Cyclic / pharmacology
Humans
Kinetics
Magnesium / pharmacology
Okadaic Acid
Phosphoprotein Phosphatases / antagonists & inhibitors
Phosphoprotein Phosphatases / metabolism*
Phosphorylation
Protein Kinases / metabolism*
Protein Phosphatase 2
Recombinant Proteins / metabolism
tau Proteins / isolation & purification
tau Proteins / metabolism*

Substances

Ethers, Cyclic
Recombinant Proteins
tau Proteins
Okadaic Acid
Protein Kinases
Calcium-Calmodulin-Dependent Protein Kinases
Phosphoprotein Phosphatases
Protein Phosphatase 2
Magnesium
Calcium