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The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM
Centrosomes comprise a pair of centrioles surrounded by a matrix of pericentriolar material (PCM). In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we inves...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Company of Biologists
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542290/ https://www.ncbi.nlm.nih.gov/pubmed/26157019 http://dx.doi.org/10.1242/bio.012914 |
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author | Richens, Jennifer H. Barros, Teresa P. Lucas, Eliana P. Peel, Nina Pinto, David Miguel Susano Wainman, Alan Raff, Jordan W. |
author_facet | Richens, Jennifer H. Barros, Teresa P. Lucas, Eliana P. Peel, Nina Pinto, David Miguel Susano Wainman, Alan Raff, Jordan W. |
author_sort | Richens, Jennifer H. |
collection | PubMed |
description | Centrosomes comprise a pair of centrioles surrounded by a matrix of pericentriolar material (PCM). In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we investigate the function of PLP during the rapid mitotic cycles of the early Drosophila embryo. Unexpectedly, we find that PLP is specifically enriched in the outer-most regions of the PCM, where it largely co-localizes with the PCM scaffold protein Cnn. In the absence of PLP the outer PCM appears to be structurally weakened, and it rapidly disperses along the centrosomal microtubules (MTs). As a result, centrosomal MTs are subtly disorganized in embryos lacking PLP, although mitosis is largely unperturbed and these embryos develop and hatch at near-normal rates. Y2H analysis reveals that PLP can potentially form multiple interactions with itself and with the PCM recruiting proteins Asl, Spd-2 and Cnn. A deletion analysis suggests that PLP participates in a complex network of interactions that ultimately help to strengthen the PCM. |
format | Online Article Text |
id | pubmed-4542290 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | The Company of Biologists |
record_format | MEDLINE/PubMed |
spelling | pubmed-45422902015-09-16 The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM Richens, Jennifer H. Barros, Teresa P. Lucas, Eliana P. Peel, Nina Pinto, David Miguel Susano Wainman, Alan Raff, Jordan W. Biol Open Research Article Centrosomes comprise a pair of centrioles surrounded by a matrix of pericentriolar material (PCM). In vertebrate cells, Pericentrin plays an important part in mitotic PCM assembly, but the Drosophila Pericentrin-like protein (PLP) appears to have a more minor role in mitotic fly cells. Here we investigate the function of PLP during the rapid mitotic cycles of the early Drosophila embryo. Unexpectedly, we find that PLP is specifically enriched in the outer-most regions of the PCM, where it largely co-localizes with the PCM scaffold protein Cnn. In the absence of PLP the outer PCM appears to be structurally weakened, and it rapidly disperses along the centrosomal microtubules (MTs). As a result, centrosomal MTs are subtly disorganized in embryos lacking PLP, although mitosis is largely unperturbed and these embryos develop and hatch at near-normal rates. Y2H analysis reveals that PLP can potentially form multiple interactions with itself and with the PCM recruiting proteins Asl, Spd-2 and Cnn. A deletion analysis suggests that PLP participates in a complex network of interactions that ultimately help to strengthen the PCM. The Company of Biologists 2015-07-08 /pmc/articles/PMC4542290/ /pubmed/26157019 http://dx.doi.org/10.1242/bio.012914 Text en © 2015. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed. |
spellingShingle | Research Article Richens, Jennifer H. Barros, Teresa P. Lucas, Eliana P. Peel, Nina Pinto, David Miguel Susano Wainman, Alan Raff, Jordan W. The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
title | The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
title_full | The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
title_fullStr | The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
title_full_unstemmed | The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
title_short | The Drosophila Pericentrin-like-protein (PLP) cooperates with Cnn to maintain the integrity of the outer PCM |
title_sort | drosophila pericentrin-like-protein (plp) cooperates with cnn to maintain the integrity of the outer pcm |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4542290/ https://www.ncbi.nlm.nih.gov/pubmed/26157019 http://dx.doi.org/10.1242/bio.012914 |
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