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Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle
Since the discovery of γ-tubulin, attention has focused on its involvement as a microtubule nucleator at the centrosome. However, mislocalization of γ-tubulin away from the centrosome does not inhibit mitotic spindle formation in Drosophila melanogaster, suggesting that a critical function for γ-tub...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2364697/ https://www.ncbi.nlm.nih.gov/pubmed/18443220 http://dx.doi.org/10.1083/jcb.200711053 |
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author | Goshima, Gohta Mayer, Mirjam Zhang, Nan Stuurman, Nico Vale, Ronald D. |
author_facet | Goshima, Gohta Mayer, Mirjam Zhang, Nan Stuurman, Nico Vale, Ronald D. |
author_sort | Goshima, Gohta |
collection | PubMed |
description | Since the discovery of γ-tubulin, attention has focused on its involvement as a microtubule nucleator at the centrosome. However, mislocalization of γ-tubulin away from the centrosome does not inhibit mitotic spindle formation in Drosophila melanogaster, suggesting that a critical function for γ-tubulin might reside elsewhere. A previous RNA interference (RNAi) screen identified five genes (Dgt2–6) required for localizing γ-tubulin to spindle microtubules. We show that the Dgt proteins interact, forming a stable complex. We find that spindle microtubule generation is substantially reduced after knockdown of each Dgt protein by RNAi. Thus, the Dgt complex that we name “augmin” functions to increase microtubule number. Reduced spindle microtubule generation after augmin RNAi, particularly in the absence of functional centrosomes, has dramatic consequences on mitotic spindle formation and function, leading to reduced kinetochore fiber formation, chromosome misalignment, and spindle bipolarity defects. We also identify a functional human homologue of Dgt6. Our results suggest that an important mitotic function for γ-tubulin may lie within the spindle, where augmin and γ-tubulin function cooperatively to amplify the number of microtubules. |
format | Text |
id | pubmed-2364697 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-23646972008-11-05 Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle Goshima, Gohta Mayer, Mirjam Zhang, Nan Stuurman, Nico Vale, Ronald D. J Cell Biol Research Articles Since the discovery of γ-tubulin, attention has focused on its involvement as a microtubule nucleator at the centrosome. However, mislocalization of γ-tubulin away from the centrosome does not inhibit mitotic spindle formation in Drosophila melanogaster, suggesting that a critical function for γ-tubulin might reside elsewhere. A previous RNA interference (RNAi) screen identified five genes (Dgt2–6) required for localizing γ-tubulin to spindle microtubules. We show that the Dgt proteins interact, forming a stable complex. We find that spindle microtubule generation is substantially reduced after knockdown of each Dgt protein by RNAi. Thus, the Dgt complex that we name “augmin” functions to increase microtubule number. Reduced spindle microtubule generation after augmin RNAi, particularly in the absence of functional centrosomes, has dramatic consequences on mitotic spindle formation and function, leading to reduced kinetochore fiber formation, chromosome misalignment, and spindle bipolarity defects. We also identify a functional human homologue of Dgt6. Our results suggest that an important mitotic function for γ-tubulin may lie within the spindle, where augmin and γ-tubulin function cooperatively to amplify the number of microtubules. The Rockefeller University Press 2008-05-05 /pmc/articles/PMC2364697/ /pubmed/18443220 http://dx.doi.org/10.1083/jcb.200711053 Text en © 2008 Goshima et al. 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.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Goshima, Gohta Mayer, Mirjam Zhang, Nan Stuurman, Nico Vale, Ronald D. Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
title | Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
title_full | Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
title_fullStr | Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
title_full_unstemmed | Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
title_short | Augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
title_sort | augmin: a protein complex required for centrosome-independent microtubule generation within the spindle |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2364697/ https://www.ncbi.nlm.nih.gov/pubmed/18443220 http://dx.doi.org/10.1083/jcb.200711053 |
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