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Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation
The centriole/basal body is a eukaryotic organelle that plays essential roles in cell division and signaling. Among five known core centriole proteins, SPD-2/Cep192 is the first recruited to the site of daughter centriole formation and regulates the centriolar localization of the other components in...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5342823/ https://www.ncbi.nlm.nih.gov/pubmed/28092264 http://dx.doi.org/10.7554/eLife.20353 |
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author | Sugioka, Kenji Hamill, Danielle R Lowry, Joshua B McNeely, Marie E Enrick, Molly Richter, Alyssa C Kiebler, Lauren E Priess, James R Bowerman, Bruce |
author_facet | Sugioka, Kenji Hamill, Danielle R Lowry, Joshua B McNeely, Marie E Enrick, Molly Richter, Alyssa C Kiebler, Lauren E Priess, James R Bowerman, Bruce |
author_sort | Sugioka, Kenji |
collection | PubMed |
description | The centriole/basal body is a eukaryotic organelle that plays essential roles in cell division and signaling. Among five known core centriole proteins, SPD-2/Cep192 is the first recruited to the site of daughter centriole formation and regulates the centriolar localization of the other components in C. elegans and in humans. However, the molecular basis for SPD-2 centriolar localization remains unknown. Here, we describe a new centriole component, the coiled-coil protein SAS-7, as a regulator of centriole duplication, assembly and elongation. Intriguingly, our genetic data suggest that SAS-7 is required for daughter centrioles to become competent for duplication, and for mother centrioles to maintain this competence. We also show that SAS-7 binds SPD-2 and regulates SPD-2 centriolar recruitment, while SAS-7 centriolar localization is SPD-2-independent. Furthermore, pericentriolar material (PCM) formation is abnormal in sas-7 mutants, and the PCM-dependent induction of cell polarity that defines the anterior-posterior body axis frequently fails. We conclude that SAS-7 functions at the earliest step in centriole duplication yet identified and plays important roles in the orchestration of centriole and PCM assembly. DOI: http://dx.doi.org/10.7554/eLife.20353.001 |
format | Online Article Text |
id | pubmed-5342823 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | eLife Sciences Publications, Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-53428232017-03-09 Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation Sugioka, Kenji Hamill, Danielle R Lowry, Joshua B McNeely, Marie E Enrick, Molly Richter, Alyssa C Kiebler, Lauren E Priess, James R Bowerman, Bruce eLife Cell Biology The centriole/basal body is a eukaryotic organelle that plays essential roles in cell division and signaling. Among five known core centriole proteins, SPD-2/Cep192 is the first recruited to the site of daughter centriole formation and regulates the centriolar localization of the other components in C. elegans and in humans. However, the molecular basis for SPD-2 centriolar localization remains unknown. Here, we describe a new centriole component, the coiled-coil protein SAS-7, as a regulator of centriole duplication, assembly and elongation. Intriguingly, our genetic data suggest that SAS-7 is required for daughter centrioles to become competent for duplication, and for mother centrioles to maintain this competence. We also show that SAS-7 binds SPD-2 and regulates SPD-2 centriolar recruitment, while SAS-7 centriolar localization is SPD-2-independent. Furthermore, pericentriolar material (PCM) formation is abnormal in sas-7 mutants, and the PCM-dependent induction of cell polarity that defines the anterior-posterior body axis frequently fails. We conclude that SAS-7 functions at the earliest step in centriole duplication yet identified and plays important roles in the orchestration of centriole and PCM assembly. DOI: http://dx.doi.org/10.7554/eLife.20353.001 eLife Sciences Publications, Ltd 2017-01-16 /pmc/articles/PMC5342823/ /pubmed/28092264 http://dx.doi.org/10.7554/eLife.20353 Text en © 2017, Sugioka et al http://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited. |
spellingShingle | Cell Biology Sugioka, Kenji Hamill, Danielle R Lowry, Joshua B McNeely, Marie E Enrick, Molly Richter, Alyssa C Kiebler, Lauren E Priess, James R Bowerman, Bruce Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation |
title | Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation |
title_full | Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation |
title_fullStr | Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation |
title_full_unstemmed | Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation |
title_short | Centriolar SAS-7 acts upstream of SPD-2 to regulate centriole assembly and pericentriolar material formation |
title_sort | centriolar sas-7 acts upstream of spd-2 to regulate centriole assembly and pericentriolar material formation |
topic | Cell Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5342823/ https://www.ncbi.nlm.nih.gov/pubmed/28092264 http://dx.doi.org/10.7554/eLife.20353 |
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