Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis
The deuterosome is a non-membranous organelle involved in large-scale centriole amplification during multiciliogenesis. Deuterosomes are specifically assembled during the process of multiciliogenesis. However, the molecular mechanisms underlying deuterosome formation are poorly understood. In this s...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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The Company of Biologists
2021-03-01
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| Series: | Biology Open |
| Subjects: | |
| Online Access: | http://bio.biologists.org/content/10/3/bio056432 |
| _version_ | 1819070422303375360 |
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| author | Shohei Yamamoto Ryoichi Yabuki Daiju Kitagawa |
| author_facet | Shohei Yamamoto Ryoichi Yabuki Daiju Kitagawa |
| author_sort | Shohei Yamamoto |
| collection | DOAJ |
| description | The deuterosome is a non-membranous organelle involved in large-scale centriole amplification during multiciliogenesis. Deuterosomes are specifically assembled during the process of multiciliogenesis. However, the molecular mechanisms underlying deuterosome formation are poorly understood. In this study, we investigated the molecular properties of deuterosome protein 1 (Deup1), an essential protein involved in deuterosome assembly. We found that Deup1 has the ability to self-assemble into macromolecular condensates both in vitro and in cells. The Deup1-containing structures formed in multiciliogenesis and the Deup1 condensates self-assembled in vitro showed low turnover of Deup1, suggesting that Deup1 forms highly stable structures. Our biochemical analyses revealed that an increase of the concentration of Deup1 and a crowded molecular environment both facilitate Deup1 self-assembly. The self-assembly of Deup1 relies on its N-terminal region, which contains multiple coiled coil domains. Using an optogenetic approach, we demonstrated that self-assembly and the C-terminal half of Deup1 were sufficient to spatially compartmentalize centrosomal protein 152 (Cep152) and polo like kinase 4 (Plk4), master components for centriole biogenesis, in the cytoplasm. Collectively, the present data suggest that Deup1 forms the structural core of the deuterosome through self-assembly into stable macromolecular condensates. This article has an associated First Person interview with the first author of the paper. |
| first_indexed | 2024-12-21T17:05:41Z |
| format | Article |
| id | doaj.art-ca52d7a3b6a24fe8b53f46f3f8d5223b |
| institution | Directory Open Access Journal |
| issn | 2046-6390 |
| language | English |
| last_indexed | 2024-12-21T17:05:41Z |
| publishDate | 2021-03-01 |
| publisher | The Company of Biologists |
| record_format | Article |
| series | Biology Open |
| spelling | doaj.art-ca52d7a3b6a24fe8b53f46f3f8d5223b2022-12-21T18:56:32ZengThe Company of BiologistsBiology Open2046-63902021-03-0110310.1242/bio.056432056432Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesisShohei Yamamoto0Ryoichi Yabuki1Daiju Kitagawa2 Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Tokyo 113-0033, Japan Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Tokyo 113-0033, Japan Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Tokyo 113-0033, Japan The deuterosome is a non-membranous organelle involved in large-scale centriole amplification during multiciliogenesis. Deuterosomes are specifically assembled during the process of multiciliogenesis. However, the molecular mechanisms underlying deuterosome formation are poorly understood. In this study, we investigated the molecular properties of deuterosome protein 1 (Deup1), an essential protein involved in deuterosome assembly. We found that Deup1 has the ability to self-assemble into macromolecular condensates both in vitro and in cells. The Deup1-containing structures formed in multiciliogenesis and the Deup1 condensates self-assembled in vitro showed low turnover of Deup1, suggesting that Deup1 forms highly stable structures. Our biochemical analyses revealed that an increase of the concentration of Deup1 and a crowded molecular environment both facilitate Deup1 self-assembly. The self-assembly of Deup1 relies on its N-terminal region, which contains multiple coiled coil domains. Using an optogenetic approach, we demonstrated that self-assembly and the C-terminal half of Deup1 were sufficient to spatially compartmentalize centrosomal protein 152 (Cep152) and polo like kinase 4 (Plk4), master components for centriole biogenesis, in the cytoplasm. Collectively, the present data suggest that Deup1 forms the structural core of the deuterosome through self-assembly into stable macromolecular condensates. This article has an associated First Person interview with the first author of the paper.http://bio.biologists.org/content/10/3/bio056432biomolecular condensatescentrioledeuterosomemulticiliogenesisself-assembly |
| spellingShingle | Shohei Yamamoto Ryoichi Yabuki Daiju Kitagawa Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis Biology Open biomolecular condensates centriole deuterosome multiciliogenesis self-assembly |
| title | Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis |
| title_full | Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis |
| title_fullStr | Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis |
| title_full_unstemmed | Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis |
| title_short | Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis |
| title_sort | biophysical and biochemical properties of deup1 self assemblies a potential driver for deuterosome formation during multiciliogenesis |
| topic | biomolecular condensates centriole deuterosome multiciliogenesis self-assembly |
| url | http://bio.biologists.org/content/10/3/bio056432 |
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