p42 map kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's disease

Michel Goedert; E. Suzanne Cohen; Ross Jakes; Philip 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

Michel Goedert
, E. Suzanne Cohen
, Ross Jakes
, Philip Cohen

Research output: Contribution to journal › Article › peer-review

284 Citations (Scopus)

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.

Original language	English
Pages (from-to)	95-99
Number of pages	5
Journal	FEBS Letters
Volume	312
Issue number	1
DOIs	https://doi.org/10.1016/0014-5793(92)81418-L
Publication status	Published - 2 Nov 1992

Keywords

Alzheimer's disease
Microtubule-associated protein tau
Mitogen-activated protein kinase
Protein phosphatase 2A

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/0014-5793(92)81418-LLicence: No Licence / Unknown

Cite this

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title = "p42 map kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's disease",

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.",

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AU - Goedert, Michel

AU - Cohen, E. Suzanne

AU - Jakes, Ross

AU - Cohen, Philip

PY - 1992/11/2

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AB - 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.

KW - Alzheimer's disease

KW - Microtubule-associated protein tau

KW - Mitogen-activated protein kinase

KW - Protein phosphatase 2A

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