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Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans

Centrosomes are important regulators of microtubule organization in animal cells. Within the centrosome, microtubule nucleation and anchorage are mediated by proteins in the pericentriolar material (PCM) that accumulates around centrioles. The spatial organization of the PCM and the contribution of...

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Autores principales: Laos, Triin, Cabral, Gabriela, Dammermann, Alexander
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cell Press 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4533240/
https://www.ncbi.nlm.nih.gov/pubmed/26241136
http://dx.doi.org/10.1016/j.cub.2015.05.060
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author Laos, Triin
Cabral, Gabriela
Dammermann, Alexander
author_facet Laos, Triin
Cabral, Gabriela
Dammermann, Alexander
author_sort Laos, Triin
collection PubMed
description Centrosomes are important regulators of microtubule organization in animal cells. Within the centrosome, microtubule nucleation and anchorage are mediated by proteins in the pericentriolar material (PCM) that accumulates around centrioles. The spatial organization of the PCM and the contribution of centrioles to its recruitment remain poorly understood. Previous work in the Drosophila embryo showed that the key PCM component Cnn specifically incorporates near centrioles, suggesting that centrioles play an ongoing role in PCM assembly [1]. It is currently unclear whether this model holds true in other organisms. Here, we examine PCM dynamics in the Caenorhabditis elegans embryo. We find that recruitment of the scaffold component SPD-5 occurs throughout the PCM. Incorporation of additional PCM subunits is therefore not limited to specific nucleation sites near centrioles, which has profound implications for the organization of the PCM lattice and the role of centrioles in centrosome assembly.
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spelling pubmed-45332402015-08-13 Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans Laos, Triin Cabral, Gabriela Dammermann, Alexander Curr Biol Correspondence Centrosomes are important regulators of microtubule organization in animal cells. Within the centrosome, microtubule nucleation and anchorage are mediated by proteins in the pericentriolar material (PCM) that accumulates around centrioles. The spatial organization of the PCM and the contribution of centrioles to its recruitment remain poorly understood. Previous work in the Drosophila embryo showed that the key PCM component Cnn specifically incorporates near centrioles, suggesting that centrioles play an ongoing role in PCM assembly [1]. It is currently unclear whether this model holds true in other organisms. Here, we examine PCM dynamics in the Caenorhabditis elegans embryo. We find that recruitment of the scaffold component SPD-5 occurs throughout the PCM. Incorporation of additional PCM subunits is therefore not limited to specific nucleation sites near centrioles, which has profound implications for the organization of the PCM lattice and the role of centrioles in centrosome assembly. Cell Press 2015-08-03 /pmc/articles/PMC4533240/ /pubmed/26241136 http://dx.doi.org/10.1016/j.cub.2015.05.060 Text en © 2015 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Correspondence
Laos, Triin
Cabral, Gabriela
Dammermann, Alexander
Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans
title Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans
title_full Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans
title_fullStr Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans
title_full_unstemmed Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans
title_short Isotropic incorporation of SPD-5 underlies centrosome assembly in C. elegans
title_sort isotropic incorporation of spd-5 underlies centrosome assembly in c. elegans
topic Correspondence
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4533240/
https://www.ncbi.nlm.nih.gov/pubmed/26241136
http://dx.doi.org/10.1016/j.cub.2015.05.060
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