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Structural organization of the dynein-dynactin complex bound to microtubules
Cytoplasmic dynein associates with dynactin to drive cargo movement on microtubules, but the structure of the dynein-dynactin complex is unknown. Using electron microscopy, we determined the organization of native bovine dynein, dynactin, and the dynein-dynactin-microtubule quaternary complex. In th...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4385409/ https://www.ncbi.nlm.nih.gov/pubmed/25751425 http://dx.doi.org/10.1038/nsmb.2996 |
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author | Chowdhury, Saikat Ketcham, Stephanie A. Schroer, Trina A. Lander, Gabriel C. |
author_facet | Chowdhury, Saikat Ketcham, Stephanie A. Schroer, Trina A. Lander, Gabriel C. |
author_sort | Chowdhury, Saikat |
collection | PubMed |
description | Cytoplasmic dynein associates with dynactin to drive cargo movement on microtubules, but the structure of the dynein-dynactin complex is unknown. Using electron microscopy, we determined the organization of native bovine dynein, dynactin, and the dynein-dynactin-microtubule quaternary complex. In the microtubule-bound complex, the dynein motor domains are positioned for processive unidirectional movement and the cargo binding domains of both dynein and dynactin are accessible. |
format | Online Article Text |
id | pubmed-4385409 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
record_format | MEDLINE/PubMed |
spelling | pubmed-43854092015-10-01 Structural organization of the dynein-dynactin complex bound to microtubules Chowdhury, Saikat Ketcham, Stephanie A. Schroer, Trina A. Lander, Gabriel C. Nat Struct Mol Biol Article Cytoplasmic dynein associates with dynactin to drive cargo movement on microtubules, but the structure of the dynein-dynactin complex is unknown. Using electron microscopy, we determined the organization of native bovine dynein, dynactin, and the dynein-dynactin-microtubule quaternary complex. In the microtubule-bound complex, the dynein motor domains are positioned for processive unidirectional movement and the cargo binding domains of both dynein and dynactin are accessible. 2015-03-09 2015-04 /pmc/articles/PMC4385409/ /pubmed/25751425 http://dx.doi.org/10.1038/nsmb.2996 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Chowdhury, Saikat Ketcham, Stephanie A. Schroer, Trina A. Lander, Gabriel C. Structural organization of the dynein-dynactin complex bound to microtubules |
title | Structural organization of the dynein-dynactin complex bound to microtubules |
title_full | Structural organization of the dynein-dynactin complex bound to microtubules |
title_fullStr | Structural organization of the dynein-dynactin complex bound to microtubules |
title_full_unstemmed | Structural organization of the dynein-dynactin complex bound to microtubules |
title_short | Structural organization of the dynein-dynactin complex bound to microtubules |
title_sort | structural organization of the dynein-dynactin complex bound to microtubules |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4385409/ https://www.ncbi.nlm.nih.gov/pubmed/25751425 http://dx.doi.org/10.1038/nsmb.2996 |
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