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Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy
High-speed atomic force microscopy was employed to observe structural changes in actin filaments induced by cofilin binding. Consistent with previous electron and fluorescence microscopic studies, cofilin formed clusters along actin filaments, where the filaments were 2-nm thicker and the helical pi...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4337605/ https://www.ncbi.nlm.nih.gov/pubmed/25642645 http://dx.doi.org/10.7554/eLife.04806 |
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author | Ngo, Kien Xuan Kodera, Noriyuki Katayama, Eisaku Ando, Toshio Uyeda, Taro QP |
author_facet | Ngo, Kien Xuan Kodera, Noriyuki Katayama, Eisaku Ando, Toshio Uyeda, Taro QP |
author_sort | Ngo, Kien Xuan |
collection | PubMed |
description | High-speed atomic force microscopy was employed to observe structural changes in actin filaments induced by cofilin binding. Consistent with previous electron and fluorescence microscopic studies, cofilin formed clusters along actin filaments, where the filaments were 2-nm thicker and the helical pitch was ∼25% shorter, compared to control filaments. Interestingly, the shortened helical pitch was propagated to the neighboring bare zone on the pointed-end side of the cluster, while the pitch on the barbed-end side was similar to the control. Thus, cofilin clusters induce distinctively asymmetric conformational changes in filaments. Consistent with the idea that cofilin favors actin structures with a shorter helical pitch, cofilin clusters grew unidirectionally toward the pointed-end of the filament. Severing was often observed near the boundaries between bare zones and clusters, but not necessarily at the boundaries. DOI: http://dx.doi.org/10.7554/eLife.04806.001 |
format | Online Article Text |
id | pubmed-4337605 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-43376052015-03-04 Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy Ngo, Kien Xuan Kodera, Noriyuki Katayama, Eisaku Ando, Toshio Uyeda, Taro QP eLife Biochemistry High-speed atomic force microscopy was employed to observe structural changes in actin filaments induced by cofilin binding. Consistent with previous electron and fluorescence microscopic studies, cofilin formed clusters along actin filaments, where the filaments were 2-nm thicker and the helical pitch was ∼25% shorter, compared to control filaments. Interestingly, the shortened helical pitch was propagated to the neighboring bare zone on the pointed-end side of the cluster, while the pitch on the barbed-end side was similar to the control. Thus, cofilin clusters induce distinctively asymmetric conformational changes in filaments. Consistent with the idea that cofilin favors actin structures with a shorter helical pitch, cofilin clusters grew unidirectionally toward the pointed-end of the filament. Severing was often observed near the boundaries between bare zones and clusters, but not necessarily at the boundaries. DOI: http://dx.doi.org/10.7554/eLife.04806.001 eLife Sciences Publications, Ltd 2015-02-02 /pmc/articles/PMC4337605/ /pubmed/25642645 http://dx.doi.org/10.7554/eLife.04806 Text en © 2015, Ngo et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Biochemistry Ngo, Kien Xuan Kodera, Noriyuki Katayama, Eisaku Ando, Toshio Uyeda, Taro QP Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
title | Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
title_full | Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
title_fullStr | Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
title_full_unstemmed | Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
title_short | Cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
title_sort | cofilin-induced unidirectional cooperative conformational changes in actin filaments revealed by high-speed atomic force microscopy |
topic | Biochemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4337605/ https://www.ncbi.nlm.nih.gov/pubmed/25642645 http://dx.doi.org/10.7554/eLife.04806 |
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