Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle

Various biological activities have been attributed to actin-capping proteins based on their in vitro effects on actin filaments. However, there is little direct evidence for their in vivo activities. In this paper, we show that Cap Z(36/32), a barbed end, actin-capping protein isolated from muscle (...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
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Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114938/
https://www.ncbi.nlm.nih.gov/pubmed/3301868
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collection PubMed
description Various biological activities have been attributed to actin-capping proteins based on their in vitro effects on actin filaments. However, there is little direct evidence for their in vivo activities. In this paper, we show that Cap Z(36/32), a barbed end, actin-capping protein isolated from muscle (Casella, J. F., D. J. Maack, and S. Lin, 1986, J. Biol. Chem., 261:10915-10921) is localized to the barbed ends of actin filaments by electron microscopy and to the Z-line of chicken skeletal muscle by indirect immunofluorescence and electron microscopy. Since actin filaments associate with the Z-line at their barbed ends, these findings suggest that Cap Z(36/32) may play a role in regulating length, orienting, or attaching actin filaments to Z-discs.
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spelling pubmed-21149382008-05-01 Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle J Cell Biol Articles Various biological activities have been attributed to actin-capping proteins based on their in vitro effects on actin filaments. However, there is little direct evidence for their in vivo activities. In this paper, we show that Cap Z(36/32), a barbed end, actin-capping protein isolated from muscle (Casella, J. F., D. J. Maack, and S. Lin, 1986, J. Biol. Chem., 261:10915-10921) is localized to the barbed ends of actin filaments by electron microscopy and to the Z-line of chicken skeletal muscle by indirect immunofluorescence and electron microscopy. Since actin filaments associate with the Z-line at their barbed ends, these findings suggest that Cap Z(36/32) may play a role in regulating length, orienting, or attaching actin filaments to Z-discs. The Rockefeller University Press 1987-07-01 /pmc/articles/PMC2114938/ /pubmed/3301868 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
Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
title Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
title_full Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
title_fullStr Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
title_full_unstemmed Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
title_short Cap Z(36/32), a barbed end actin-capping protein, is a component of the Z-line of skeletal muscle
title_sort cap z(36/32), a barbed end actin-capping protein, is a component of the z-line of skeletal muscle
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114938/
https://www.ncbi.nlm.nih.gov/pubmed/3301868

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