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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...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1980
Materias:
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.
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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