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Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans

Augmin is a protein complex that binds to spindle microtubules (MTs), recruits the potent MT nucleator, γ-tubulin, and thereby promotes the centrosome-independent MT generation within mitotic and meiotic spindles. Augmin is essential for acentrosomal spindle assembly, which is commonly observed duri...

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Autores principales: Edzuka, Tomoya, Yamada, Lixy, Kanamaru, Kyoko, Sawada, Hitoshi, Goshima, Gohta
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086812/
https://www.ncbi.nlm.nih.gov/pubmed/25003582
http://dx.doi.org/10.1371/journal.pone.0101471
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author Edzuka, Tomoya
Yamada, Lixy
Kanamaru, Kyoko
Sawada, Hitoshi
Goshima, Gohta
author_facet Edzuka, Tomoya
Yamada, Lixy
Kanamaru, Kyoko
Sawada, Hitoshi
Goshima, Gohta
author_sort Edzuka, Tomoya
collection PubMed
description Augmin is a protein complex that binds to spindle microtubules (MTs), recruits the potent MT nucleator, γ-tubulin, and thereby promotes the centrosome-independent MT generation within mitotic and meiotic spindles. Augmin is essential for acentrosomal spindle assembly, which is commonly observed during mitosis in plants and meiosis in female animals. In many animal somatic cells that possess centrosomes, the centrosome- and augmin-dependent mechanisms work cooperatively for efficient spindle assembly and cytokinesis. Yeasts have lost the augmin genes during evolution. It is hypothesized that their robust MT nucleation from the spindle pole body (SPB), the centrosome-equivalent structure in fungi, compensates for the lack of augmin. Intriguingly, however, a gene homologous to an augmin subunit (Aug6/AUGF) has been found in the genome of filamentous fungi, which has the SPB as a robust MT nucleation centre. Here, we aimed to clarify if the augmin complex is present in filamentous fungi and to identify its role in mitosis. By analysing the Aug6-like gene in the filamentous fungus Aspergillus nidulans, we found that it forms a large complex with several other proteins that share weak but significant homology to known augmin subunits. In A. nidulans, augmin was enriched at the SPB and also associated with spindle MTs during mitosis. However, the augmin gene disruptants did not exhibit growth defects under normal, checkpoint-deficient, or MT-destabilised conditions. Moreover, we obtained no evidence that A. nidulans augmin plays a role in γ-tubulin recruitment or in mitotic cell division. Our study uncovered the conservation of the augmin complex in the fungal species, and further suggests that augmin has several functions, besides mitotic spindle MT nucleation, that are yet to be identified.
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spelling pubmed-40868122014-07-14 Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans Edzuka, Tomoya Yamada, Lixy Kanamaru, Kyoko Sawada, Hitoshi Goshima, Gohta PLoS One Research Article Augmin is a protein complex that binds to spindle microtubules (MTs), recruits the potent MT nucleator, γ-tubulin, and thereby promotes the centrosome-independent MT generation within mitotic and meiotic spindles. Augmin is essential for acentrosomal spindle assembly, which is commonly observed during mitosis in plants and meiosis in female animals. In many animal somatic cells that possess centrosomes, the centrosome- and augmin-dependent mechanisms work cooperatively for efficient spindle assembly and cytokinesis. Yeasts have lost the augmin genes during evolution. It is hypothesized that their robust MT nucleation from the spindle pole body (SPB), the centrosome-equivalent structure in fungi, compensates for the lack of augmin. Intriguingly, however, a gene homologous to an augmin subunit (Aug6/AUGF) has been found in the genome of filamentous fungi, which has the SPB as a robust MT nucleation centre. Here, we aimed to clarify if the augmin complex is present in filamentous fungi and to identify its role in mitosis. By analysing the Aug6-like gene in the filamentous fungus Aspergillus nidulans, we found that it forms a large complex with several other proteins that share weak but significant homology to known augmin subunits. In A. nidulans, augmin was enriched at the SPB and also associated with spindle MTs during mitosis. However, the augmin gene disruptants did not exhibit growth defects under normal, checkpoint-deficient, or MT-destabilised conditions. Moreover, we obtained no evidence that A. nidulans augmin plays a role in γ-tubulin recruitment or in mitotic cell division. Our study uncovered the conservation of the augmin complex in the fungal species, and further suggests that augmin has several functions, besides mitotic spindle MT nucleation, that are yet to be identified. Public Library of Science 2014-07-08 /pmc/articles/PMC4086812/ /pubmed/25003582 http://dx.doi.org/10.1371/journal.pone.0101471 Text en © 2014 Edzuka et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Edzuka, Tomoya
Yamada, Lixy
Kanamaru, Kyoko
Sawada, Hitoshi
Goshima, Gohta
Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans
title Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans
title_full Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans
title_fullStr Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans
title_full_unstemmed Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans
title_short Identification of the Augmin Complex in the Filamentous Fungus Aspergillus nidulans
title_sort identification of the augmin complex in the filamentous fungus aspergillus nidulans
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4086812/
https://www.ncbi.nlm.nih.gov/pubmed/25003582
http://dx.doi.org/10.1371/journal.pone.0101471
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