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PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation
Abnormal amplification of centrosomes could lead to improper chromosome segregation and aneuploidy and is implicated in cancer development. Here, we demonstrate that Axin, a scaffolding protein in Wnt signaling, is phosphorylated by PLK1 during mitosis. Phosphorylation of Axin Ser-157 by PLK1 abolis...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498349/ https://www.ncbi.nlm.nih.gov/pubmed/23155463 http://dx.doi.org/10.1371/journal.pone.0049184 |
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author | Ruan, Ka Ye, Fan Li, Chenyu Liou, Yih-Cherng Lin, Sheng-Cai Lin, Shu-Yong |
author_facet | Ruan, Ka Ye, Fan Li, Chenyu Liou, Yih-Cherng Lin, Sheng-Cai Lin, Shu-Yong |
author_sort | Ruan, Ka |
collection | PubMed |
description | Abnormal amplification of centrosomes could lead to improper chromosome segregation and aneuploidy and is implicated in cancer development. Here, we demonstrate that Axin, a scaffolding protein in Wnt signaling, is phosphorylated by PLK1 during mitosis. Phosphorylation of Axin Ser-157 by PLK1 abolished Axin association with γ-tubulin, while substitution of Ser-157 with alanine exhibited sustained interaction with γ-tubulin. In addition, overexpression of Axin-S157A significantly increased the number of cells with multi-centrosomes. These results suggest that the phosphorylation status of Axin, mediated by PLK1, dynamically regulates its association with γ-tubulin and centrosome formation and segregation. |
format | Online Article Text |
id | pubmed-3498349 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-34983492012-11-15 PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation Ruan, Ka Ye, Fan Li, Chenyu Liou, Yih-Cherng Lin, Sheng-Cai Lin, Shu-Yong PLoS One Research Article Abnormal amplification of centrosomes could lead to improper chromosome segregation and aneuploidy and is implicated in cancer development. Here, we demonstrate that Axin, a scaffolding protein in Wnt signaling, is phosphorylated by PLK1 during mitosis. Phosphorylation of Axin Ser-157 by PLK1 abolished Axin association with γ-tubulin, while substitution of Ser-157 with alanine exhibited sustained interaction with γ-tubulin. In addition, overexpression of Axin-S157A significantly increased the number of cells with multi-centrosomes. These results suggest that the phosphorylation status of Axin, mediated by PLK1, dynamically regulates its association with γ-tubulin and centrosome formation and segregation. Public Library of Science 2012-11-14 /pmc/articles/PMC3498349/ /pubmed/23155463 http://dx.doi.org/10.1371/journal.pone.0049184 Text en © 2012 Ruan et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ruan, Ka Ye, Fan Li, Chenyu Liou, Yih-Cherng Lin, Sheng-Cai Lin, Shu-Yong PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation |
title | PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation |
title_full | PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation |
title_fullStr | PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation |
title_full_unstemmed | PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation |
title_short | PLK1 Interacts and Phosphorylates Axin That Is Essential for Proper Centrosome Formation |
title_sort | plk1 interacts and phosphorylates axin that is essential for proper centrosome formation |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3498349/ https://www.ncbi.nlm.nih.gov/pubmed/23155463 http://dx.doi.org/10.1371/journal.pone.0049184 |
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