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PMID: 2507554 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation.

The Journal of cell biology ·Vol. 109 ·No. 4 Pt 1 ·1989-10-00 ·Pages 1643-51

Hagestedt T, Lichtenberg B, Wille H, Mandelkow EM, Mandelkow E

Abstract

In a previous report we have shown that microtubule-associated protein tau can be induced to form paracrystals (Lichtenberg, B., E.-M. Mandelkow, T. Hagestedt, and E. Mandelkow. 1988. Nature [Lond.]. 334:359-362). A striking feature was the high degree of elasticity of the molecules. We now report that this property is related to the state of phosphorylation. When tau is dephosphorylated by alkaline phosphatase, it becomes shorter and more elastic; when it is phosphorylated by Ca++/calmodulin-dependent kinase, it becomes longer and stiffer. This may provide a model for the control of structural properties of tau-like molecules by phosphorylation.

MeSH Terms
Animals Brain/metabolism Crystallization Elasticity Microscopy, Electron Microtubule-Associated Proteins/isolation & purification,metabolism Microtubules/metabolism Molecular Weight Nerve Tissue Proteins/metabolism Phosphorylation Protein Conformation Swine tau Proteins
Chemicals
Microtubule-Associated Proteins Nerve Tissue Proteins tau Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Hagestedt T
Max Planck Unit for Structural Molecular Biology, Hamburg, Federal Republic of Germany.
Lichtenberg B
Wille H
Mandelkow E M
Mandelkow E
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.109.4.1643
Published
1989-10-00
Pages
1643-51
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2115827
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.109.4.1643 PMC Full Text View journal details
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