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Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae
Recent research in filamentous fungi has revealed that the motility of an endocytic organelle early endosome (EE) has a versatile role in many physiological functions. Here, to further examine the motility of EEs in the industrially important fungus Aspergillus oryzae, we visualized these organelles...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5693997/ https://www.ncbi.nlm.nih.gov/pubmed/29150640 http://dx.doi.org/10.1038/s41598-017-16163-1 |
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author | Togo, Yusuke Higuchi, Yujiro Katakura, Yoshinori Takegawa, Kaoru |
author_facet | Togo, Yusuke Higuchi, Yujiro Katakura, Yoshinori Takegawa, Kaoru |
author_sort | Togo, Yusuke |
collection | PubMed |
description | Recent research in filamentous fungi has revealed that the motility of an endocytic organelle early endosome (EE) has a versatile role in many physiological functions. Here, to further examine the motility of EEs in the industrially important fungus Aspergillus oryzae, we visualized these organelles via the Rab5 homolog AoRab5 and identified AoHok1, a putative linker protein between an EE and a motor protein. The Aohok1 disruptant showed retarded mycelial growth and no EE motility, in addition to an apical accumulation of EEs and peroxisomes. We further demonstrated that the Aohok1 disruptant exhibited less sensitivity to osmotic and cell wall stresses. Analyses on the protein secretory pathway in ΔAohok1 cells showed that, although distribution of the endoplasmic reticulum and Golgi was not affected, formation of the apical secretory vesicle cluster Spitzenkörper was impaired, probably resulting in the observed reduction of the A. oryzae major secretory protein α-amylase. Moreover, we revealed that the transcript level of α-amylase-encoding gene amyB was significantly reduced in the Aohok1 disruptant. Furthermore, we observed perturbed conidial and sclerotial formations, indicating a defect in cell differentiation, in the Aohok1 disruptant. Collectively, our results suggest that EE motility is crucial for α-amylase production and cell differentiation in A. oryzae. |
format | Online Article Text |
id | pubmed-5693997 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-56939972017-11-27 Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae Togo, Yusuke Higuchi, Yujiro Katakura, Yoshinori Takegawa, Kaoru Sci Rep Article Recent research in filamentous fungi has revealed that the motility of an endocytic organelle early endosome (EE) has a versatile role in many physiological functions. Here, to further examine the motility of EEs in the industrially important fungus Aspergillus oryzae, we visualized these organelles via the Rab5 homolog AoRab5 and identified AoHok1, a putative linker protein between an EE and a motor protein. The Aohok1 disruptant showed retarded mycelial growth and no EE motility, in addition to an apical accumulation of EEs and peroxisomes. We further demonstrated that the Aohok1 disruptant exhibited less sensitivity to osmotic and cell wall stresses. Analyses on the protein secretory pathway in ΔAohok1 cells showed that, although distribution of the endoplasmic reticulum and Golgi was not affected, formation of the apical secretory vesicle cluster Spitzenkörper was impaired, probably resulting in the observed reduction of the A. oryzae major secretory protein α-amylase. Moreover, we revealed that the transcript level of α-amylase-encoding gene amyB was significantly reduced in the Aohok1 disruptant. Furthermore, we observed perturbed conidial and sclerotial formations, indicating a defect in cell differentiation, in the Aohok1 disruptant. Collectively, our results suggest that EE motility is crucial for α-amylase production and cell differentiation in A. oryzae. Nature Publishing Group UK 2017-11-17 /pmc/articles/PMC5693997/ /pubmed/29150640 http://dx.doi.org/10.1038/s41598-017-16163-1 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Togo, Yusuke Higuchi, Yujiro Katakura, Yoshinori Takegawa, Kaoru Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae |
title | Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae |
title_full | Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae |
title_fullStr | Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae |
title_full_unstemmed | Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae |
title_short | Early endosome motility mediates α-amylase production and cell differentiation in Aspergillus oryzae |
title_sort | early endosome motility mediates α-amylase production and cell differentiation in aspergillus oryzae |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5693997/ https://www.ncbi.nlm.nih.gov/pubmed/29150640 http://dx.doi.org/10.1038/s41598-017-16163-1 |
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