Cargando…
Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation
The centrosomal pericentrin-related proteins play pivotal roles in various aspects of cell division; however their underlying mechanisms remain largely elusive. Here we show that fission-yeast pericentrin-like Pcp1 regulates multiple functions of the spindle pole body (SPB) through recruiting two cr...
Autores principales: | , , |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788132/ https://www.ncbi.nlm.nih.gov/pubmed/19942852 http://dx.doi.org/10.1038/emboj.2009.331 |
_version_ | 1782174932026785792 |
---|---|
author | Fong, Chii Shyang Sato, Masamitsu Toda, Takashi |
author_facet | Fong, Chii Shyang Sato, Masamitsu Toda, Takashi |
author_sort | Fong, Chii Shyang |
collection | PubMed |
description | The centrosomal pericentrin-related proteins play pivotal roles in various aspects of cell division; however their underlying mechanisms remain largely elusive. Here we show that fission-yeast pericentrin-like Pcp1 regulates multiple functions of the spindle pole body (SPB) through recruiting two critical factors, the γ-tubulin complex (γ-TuC) and polo kinase (Plo1). We isolated two pcp1 mutants (pcp1-15 and pcp1-18) that display similar abnormal spindles, but with remarkably different molecular defects. Both mutants exhibit defective monopolar spindle microtubules that emanate from the mother SPB. However, while pcp1-15 fails to localise the γ-TuC to the mitotic SPB, pcp1-18 is specifically defective in recruiting Plo1. Consistently Pcp1 forms a complex with both γ-TuC and Plo1 in the cell. pcp1-18 is further defective in the mitotic-specific reorganisation of the nuclear envelope (NE), leading to impairment of SPB insertion into the NE. Moreover pcp1-18, but not pcp1-15, is rescued by overproducing nuclear pore components or advancing mitotic onset. The central role for Pcp1 in orchestrating these processes provides mechanistic insight into how the centrosome regulates multiple cellular pathways. |
format | Text |
id | pubmed-2788132 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-27881322009-12-03 Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation Fong, Chii Shyang Sato, Masamitsu Toda, Takashi EMBO J Article The centrosomal pericentrin-related proteins play pivotal roles in various aspects of cell division; however their underlying mechanisms remain largely elusive. Here we show that fission-yeast pericentrin-like Pcp1 regulates multiple functions of the spindle pole body (SPB) through recruiting two critical factors, the γ-tubulin complex (γ-TuC) and polo kinase (Plo1). We isolated two pcp1 mutants (pcp1-15 and pcp1-18) that display similar abnormal spindles, but with remarkably different molecular defects. Both mutants exhibit defective monopolar spindle microtubules that emanate from the mother SPB. However, while pcp1-15 fails to localise the γ-TuC to the mitotic SPB, pcp1-18 is specifically defective in recruiting Plo1. Consistently Pcp1 forms a complex with both γ-TuC and Plo1 in the cell. pcp1-18 is further defective in the mitotic-specific reorganisation of the nuclear envelope (NE), leading to impairment of SPB insertion into the NE. Moreover pcp1-18, but not pcp1-15, is rescued by overproducing nuclear pore components or advancing mitotic onset. The central role for Pcp1 in orchestrating these processes provides mechanistic insight into how the centrosome regulates multiple cellular pathways. Nature Publishing Group 2010-01-06 2009-11-26 /pmc/articles/PMC2788132/ /pubmed/19942852 http://dx.doi.org/10.1038/emboj.2009.331 Text en Copyright © 2009, European Molecular Biology Organization http://creativecommons.org/licenses/by-nc-sa/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits distribution, and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation without specific permission. |
spellingShingle | Article Fong, Chii Shyang Sato, Masamitsu Toda, Takashi Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
title | Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
title_full | Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
title_fullStr | Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
title_full_unstemmed | Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
title_short | Fission yeast Pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
title_sort | fission yeast pcp1 links polo kinase-mediated mitotic entry to γ-tubulin-dependent spindle formation |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2788132/ https://www.ncbi.nlm.nih.gov/pubmed/19942852 http://dx.doi.org/10.1038/emboj.2009.331 |
work_keys_str_mv | AT fongchiishyang fissionyeastpcp1linkspolokinasemediatedmitoticentrytogtubulindependentspindleformation AT satomasamitsu fissionyeastpcp1linkspolokinasemediatedmitoticentrytogtubulindependentspindleformation AT todatakashi fissionyeastpcp1linkspolokinasemediatedmitoticentrytogtubulindependentspindleformation |