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

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 t...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1989
Materias:
Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115827/
https://www.ncbi.nlm.nih.gov/pubmed/2507554
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collection PubMed
description 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.
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spelling pubmed-21158272008-05-01 Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation J Cell Biol Articles 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. The Rockefeller University Press 1989-10-01 /pmc/articles/PMC2115827/ /pubmed/2507554 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
title Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
title_full Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
title_fullStr Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
title_full_unstemmed Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
title_short Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
title_sort tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115827/
https://www.ncbi.nlm.nih.gov/pubmed/2507554

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