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PMID: 1644173 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs.

FEBS letters ·Vol. 307 ·No. 2 ·1992-07-28 ·Pages 199-205

Gustke N, Steiner B, Mandelkow EM, Biernat J, Meyer HE, Goedert M, Mandelkow E

Abstract

Tau protein can be transformed into an Alzheimer-like state by phosphorylation with a kinase activity from brain [Biernat et al. (1992) EMBO J. 11, 1593-1597]. Here we show that the phosphorylation at Ser-Pro motifs strongly decreases tau's affinity for microtubules. The major reduction occurs during the first of the three main stages of phosphorylation. The data explain the lower stability of microtubules resulting from the pathological tau phosphorylation.

MeSH Terms

Alzheimer Disease/metabolism Amino Acid Sequence Brain/metabolism Chromatography, High Pressure Liquid Electrophoresis, Polyacrylamide Gel Humans Microtubules/metabolism Molecular Sequence Data Mutation Phosphorylation Proline/metabolism Protein Binding Protein Kinases/metabolism Serine/metabolism Threonine/metabolism tau Proteins/chemistry,metabolism

Chemicals

tau Proteins Threonine Serine Proline Protein Kinases

Authors & Affiliations

7 authors, click to expand affiliations / ORCID

Gustke N

Max-Planck-Unit for Structural Molecular Biology, c/o DESY, Hamburg, Germany.

Steiner B

Mandelkow E M

Biernat J

Meyer H E

Goedert M

Mandelkow E

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(92)80767-b

Published

1992-07-28

Pages

199-205

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(92)80767-b View journal details

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The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs.

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