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Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis
Lis1, Nudel/NudE, and dynactin are regulators of cytoplasmic dynein, a minus end–directed, microtubule (MT)-based motor required for proper spindle assembly and orientation. In vitro studies have shown that dynactin promotes processive movement of dynein on MTs, whereas Lis1 causes dynein to enter a...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3826990/ https://www.ncbi.nlm.nih.gov/pubmed/24025714 http://dx.doi.org/10.1091/mbc.E13-05-0283 |
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author | Wang, Shusheng Ketcham, Stephanie A. Schön, Arne Goodman, Benjamin Wang, Yueju Yates, John Freire, Ernesto Schroer, Trina A. Zheng, Yixian |
author_facet | Wang, Shusheng Ketcham, Stephanie A. Schön, Arne Goodman, Benjamin Wang, Yueju Yates, John Freire, Ernesto Schroer, Trina A. Zheng, Yixian |
author_sort | Wang, Shusheng |
collection | PubMed |
description | Lis1, Nudel/NudE, and dynactin are regulators of cytoplasmic dynein, a minus end–directed, microtubule (MT)-based motor required for proper spindle assembly and orientation. In vitro studies have shown that dynactin promotes processive movement of dynein on MTs, whereas Lis1 causes dynein to enter a persistent force-generating state (referred to here as dynein stall). Yet how the activities of Lis1, Nudel/NudE, and dynactin are coordinated to regulate dynein remains poorly understood in vivo. Working in Xenopus egg extracts, we show that Nudel/NudE facilitates the binding of Lis1 to dynein, which enhances the recruitment of dynactin to dynein. We further report a novel Lis1-dependent dynein–dynactin interaction that is essential for the organization of mitotic spindle poles. Finally, using assays for MT gliding and spindle assembly, we demonstrate an antagonistic relationship between Lis1 and dynactin that allows dynactin to relieve Lis1-induced dynein stall on MTs. Our findings suggest the interesting possibility that Lis1 and dynactin could alternately engage with dynein to allow the motor to promote spindle assembly. |
format | Online Article Text |
id | pubmed-3826990 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-38269902014-01-30 Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis Wang, Shusheng Ketcham, Stephanie A. Schön, Arne Goodman, Benjamin Wang, Yueju Yates, John Freire, Ernesto Schroer, Trina A. Zheng, Yixian Mol Biol Cell Articles Lis1, Nudel/NudE, and dynactin are regulators of cytoplasmic dynein, a minus end–directed, microtubule (MT)-based motor required for proper spindle assembly and orientation. In vitro studies have shown that dynactin promotes processive movement of dynein on MTs, whereas Lis1 causes dynein to enter a persistent force-generating state (referred to here as dynein stall). Yet how the activities of Lis1, Nudel/NudE, and dynactin are coordinated to regulate dynein remains poorly understood in vivo. Working in Xenopus egg extracts, we show that Nudel/NudE facilitates the binding of Lis1 to dynein, which enhances the recruitment of dynactin to dynein. We further report a novel Lis1-dependent dynein–dynactin interaction that is essential for the organization of mitotic spindle poles. Finally, using assays for MT gliding and spindle assembly, we demonstrate an antagonistic relationship between Lis1 and dynactin that allows dynactin to relieve Lis1-induced dynein stall on MTs. Our findings suggest the interesting possibility that Lis1 and dynactin could alternately engage with dynein to allow the motor to promote spindle assembly. The American Society for Cell Biology 2013-11-15 /pmc/articles/PMC3826990/ /pubmed/24025714 http://dx.doi.org/10.1091/mbc.E13-05-0283 Text en © 2013 Wang et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Wang, Shusheng Ketcham, Stephanie A. Schön, Arne Goodman, Benjamin Wang, Yueju Yates, John Freire, Ernesto Schroer, Trina A. Zheng, Yixian Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
title | Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
title_full | Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
title_fullStr | Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
title_full_unstemmed | Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
title_short | Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
title_sort | nudel/nude and lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3826990/ https://www.ncbi.nlm.nih.gov/pubmed/24025714 http://dx.doi.org/10.1091/mbc.E13-05-0283 |
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