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Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments
Branching filaments with striking perpendicularity form when actin polymerizes in the presence of macrophage actin-binding protein. Actin- binding protein molecules are visible at the branch points. Compared with actin polymerized in the absence of actin-binding proteins, not only do the filaments b...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1980
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110793/ https://www.ncbi.nlm.nih.gov/pubmed/6893990 |
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collection | PubMed |
description | Branching filaments with striking perpendicularity form when actin polymerizes in the presence of macrophage actin-binding protein. Actin- binding protein molecules are visible at the branch points. Compared with actin polymerized in the absence of actin-binding proteins, not only do the filaments branch but the average length of the actin filaments decreases from 3.2 to 0.63 micrometer. Arrowhead complexes formed by addition of heavy meromyosin molecules to the branching actin filaments point toward the branch points. Actin-binding protein also accelerates the onset of actin polymerization. All of these findings show that actin filaments assemble from nucleating sites on actin- binding protein dimers. A branching polymerization of actin filaments from a preexisting lattice of actin filaments joined by actin-binding protein molecules could generate expansion of cortical cytoplasm in amoeboid cells. |
format | Text |
id | pubmed-2110793 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1980 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21107932008-05-01 Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments J Cell Biol Articles Branching filaments with striking perpendicularity form when actin polymerizes in the presence of macrophage actin-binding protein. Actin- binding protein molecules are visible at the branch points. Compared with actin polymerized in the absence of actin-binding proteins, not only do the filaments branch but the average length of the actin filaments decreases from 3.2 to 0.63 micrometer. Arrowhead complexes formed by addition of heavy meromyosin molecules to the branching actin filaments point toward the branch points. Actin-binding protein also accelerates the onset of actin polymerization. All of these findings show that actin filaments assemble from nucleating sites on actin- binding protein dimers. A branching polymerization of actin filaments from a preexisting lattice of actin filaments joined by actin-binding protein molecules could generate expansion of cortical cytoplasm in amoeboid cells. The Rockefeller University Press 1980-12-01 /pmc/articles/PMC2110793/ /pubmed/6893990 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 Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
title | Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
title_full | Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
title_fullStr | Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
title_full_unstemmed | Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
title_short | Actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
title_sort | actin-binding protein promotes the bipolar and perpendicular branching of actin filaments |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110793/ https://www.ncbi.nlm.nih.gov/pubmed/6893990 |