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Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins

We have used low shear viscometry and electron microscopy to study the interaction between pure actin filaments and microtubules. Mixtures of microtubules having microtubule-associated proteins (MAPs) with actin filament have very high viscosities compared with the viscosities of the separate compon...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1978
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110189/
https://www.ncbi.nlm.nih.gov/pubmed/568144
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collection PubMed
description We have used low shear viscometry and electron microscopy to study the interaction between pure actin filaments and microtubules. Mixtures of microtubules having microtubule-associated proteins (MAPs) with actin filament have very high viscosities compared with the viscosities of the separate components. MAPs themselves also cause a large increase in the viscosity of actin filaments. In contrast, mixtures of actin filaments with tubulin polymers lacking MAPs have low viscosities, close to the sum of the viscosities of the separate components. Our interpretation of these observations is that there is an interaction between actin filaments and microtubules which requires MAPs. This interaction is inhibited by ATP and some related compounds. Electron micrographs of thin sections through mixtures of actin and microtubules show numerous close associations between the two polymers which may be responsible for their high viscosity.
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spelling pubmed-21101892008-05-01 Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins J Cell Biol Articles We have used low shear viscometry and electron microscopy to study the interaction between pure actin filaments and microtubules. Mixtures of microtubules having microtubule-associated proteins (MAPs) with actin filament have very high viscosities compared with the viscosities of the separate components. MAPs themselves also cause a large increase in the viscosity of actin filaments. In contrast, mixtures of actin filaments with tubulin polymers lacking MAPs have low viscosities, close to the sum of the viscosities of the separate components. Our interpretation of these observations is that there is an interaction between actin filaments and microtubules which requires MAPs. This interaction is inhibited by ATP and some related compounds. Electron micrographs of thin sections through mixtures of actin and microtubules show numerous close associations between the two polymers which may be responsible for their high viscosity. The Rockefeller University Press 1978-09-01 /pmc/articles/PMC2110189/ /pubmed/568144 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
Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
title Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
title_full Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
title_fullStr Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
title_full_unstemmed Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
title_short Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
title_sort evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110189/
https://www.ncbi.nlm.nih.gov/pubmed/568144