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Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly
Centriolar satellites are numerous electron-dense granules dispersed around the centrosome. Mutations in their components are linked to various human diseases, but their molecular roles remain elusive. In particular, the significance of spatial communication between centriolar satellites and the cen...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4472012/ https://www.ncbi.nlm.nih.gov/pubmed/25833712 http://dx.doi.org/10.1091/mbc.E14-11-1561 |
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author | Hori, Akiko Peddie, Christopher J. Collinson, Lucy M. Toda, Takashi |
author_facet | Hori, Akiko Peddie, Christopher J. Collinson, Lucy M. Toda, Takashi |
author_sort | Hori, Akiko |
collection | PubMed |
description | Centriolar satellites are numerous electron-dense granules dispersed around the centrosome. Mutations in their components are linked to various human diseases, but their molecular roles remain elusive. In particular, the significance of spatial communication between centriolar satellites and the centrosome is unknown. hMsd1/SSX2IP localizes to both the centrosome and centriolar satellites and is required for tethering microtubules to the centrosome. Here we show that hMsd1/SSX2IP-mediated microtubule anchoring is essential for proper centriole assembly and duplication. On hMsd1/SSX2IP knockdown, the centriolar satellites become stuck at the microtubule minus end near the centrosome. Intriguingly, these satellites contain many proteins that normally localize to the centrosome. Of importance, microtubule structures, albeit not being anchored properly, are still required for the emergence of abnormal satellites, as complete microtubule depolymerization results in the disappearance of these aggregates from the vicinity of the centrosome. We highlighted, using superresolution and electron microscopy, that under these conditions, centriole structures are faulty. Remarkably, these cells are insensitive to Plk4 overproduction–induced ectopic centriole formation, yet they accelerate centrosome reduplication upon hydroxyurea arrest. Finally, the appearance of satellite aggregates is cancer cell specific. Together our findings provide novel insights into the mechanism of centriole assembly and microtubule anchoring. |
format | Online Article Text |
id | pubmed-4472012 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-44720122015-08-16 Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly Hori, Akiko Peddie, Christopher J. Collinson, Lucy M. Toda, Takashi Mol Biol Cell Articles Centriolar satellites are numerous electron-dense granules dispersed around the centrosome. Mutations in their components are linked to various human diseases, but their molecular roles remain elusive. In particular, the significance of spatial communication between centriolar satellites and the centrosome is unknown. hMsd1/SSX2IP localizes to both the centrosome and centriolar satellites and is required for tethering microtubules to the centrosome. Here we show that hMsd1/SSX2IP-mediated microtubule anchoring is essential for proper centriole assembly and duplication. On hMsd1/SSX2IP knockdown, the centriolar satellites become stuck at the microtubule minus end near the centrosome. Intriguingly, these satellites contain many proteins that normally localize to the centrosome. Of importance, microtubule structures, albeit not being anchored properly, are still required for the emergence of abnormal satellites, as complete microtubule depolymerization results in the disappearance of these aggregates from the vicinity of the centrosome. We highlighted, using superresolution and electron microscopy, that under these conditions, centriole structures are faulty. Remarkably, these cells are insensitive to Plk4 overproduction–induced ectopic centriole formation, yet they accelerate centrosome reduplication upon hydroxyurea arrest. Finally, the appearance of satellite aggregates is cancer cell specific. Together our findings provide novel insights into the mechanism of centriole assembly and microtubule anchoring. The American Society for Cell Biology 2015-06-01 /pmc/articles/PMC4472012/ /pubmed/25833712 http://dx.doi.org/10.1091/mbc.E14-11-1561 Text en © 2015 Hori 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 for Cell Biology. |
spellingShingle | Articles Hori, Akiko Peddie, Christopher J. Collinson, Lucy M. Toda, Takashi Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly |
title | Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly |
title_full | Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly |
title_fullStr | Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly |
title_full_unstemmed | Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly |
title_short | Centriolar satellite– and hMsd1/SSX2IP-dependent microtubule anchoring is critical for centriole assembly |
title_sort | centriolar satellite– and hmsd1/ssx2ip-dependent microtubule anchoring is critical for centriole assembly |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4472012/ https://www.ncbi.nlm.nih.gov/pubmed/25833712 http://dx.doi.org/10.1091/mbc.E14-11-1561 |
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