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MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes
The interplay between maturation-promoting factor (MPF), mitogen-activated protein kinase (MAPK) and Rho GTPase during actin-myosin interactions has yet to be determined. The mechanism by which microtubule disrupters induce the formation of ooplasmic protrusion during chemical-assisted enucleation o...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2938347/ https://www.ncbi.nlm.nih.gov/pubmed/20856880 http://dx.doi.org/10.1371/journal.pone.0012706 |
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author | Wu, Yan-Guang Zhou, Ping Lan, Guo-Cheng Gao, Da Li, Qing Wei, De-Li Wang, Hui-Li Tan, Jing-He |
author_facet | Wu, Yan-Guang Zhou, Ping Lan, Guo-Cheng Gao, Da Li, Qing Wei, De-Li Wang, Hui-Li Tan, Jing-He |
author_sort | Wu, Yan-Guang |
collection | PubMed |
description | The interplay between maturation-promoting factor (MPF), mitogen-activated protein kinase (MAPK) and Rho GTPase during actin-myosin interactions has yet to be determined. The mechanism by which microtubule disrupters induce the formation of ooplasmic protrusion during chemical-assisted enucleation of mammalian oocytes is unknown. Moreover, a suitable model is urgently needed for the study of cytokinesis. We have established a model of chemical-induced cytokinesis and have studied the signaling events leading to cytokinesis using this model. The results suggested that microtubule inhibitors activated MPF, which induced actomyosin assembly (formation of ooplasmic protrusion) by activating RhoA and thus MAPK. While MAPK controlled actin recruitment on its own, MPF promoted myosin enrichment by activating RhoA and MAPK. A further chemical treatment of oocytes with protrusions induced constriction of the actomyosin ring by inactivating MPF while activating RhoA. In conclusion, the present data suggested that the assembly and contraction of the actomyosin ring were two separable steps: while an increase in MPF activity promoted the assembly through RhoA-mediated activation of MAPK, a decrease in MPF activity triggered contraction of the ring by activating RhoA. |
format | Text |
id | pubmed-2938347 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-29383472010-09-20 MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes Wu, Yan-Guang Zhou, Ping Lan, Guo-Cheng Gao, Da Li, Qing Wei, De-Li Wang, Hui-Li Tan, Jing-He PLoS One Research Article The interplay between maturation-promoting factor (MPF), mitogen-activated protein kinase (MAPK) and Rho GTPase during actin-myosin interactions has yet to be determined. The mechanism by which microtubule disrupters induce the formation of ooplasmic protrusion during chemical-assisted enucleation of mammalian oocytes is unknown. Moreover, a suitable model is urgently needed for the study of cytokinesis. We have established a model of chemical-induced cytokinesis and have studied the signaling events leading to cytokinesis using this model. The results suggested that microtubule inhibitors activated MPF, which induced actomyosin assembly (formation of ooplasmic protrusion) by activating RhoA and thus MAPK. While MAPK controlled actin recruitment on its own, MPF promoted myosin enrichment by activating RhoA and MAPK. A further chemical treatment of oocytes with protrusions induced constriction of the actomyosin ring by inactivating MPF while activating RhoA. In conclusion, the present data suggested that the assembly and contraction of the actomyosin ring were two separable steps: while an increase in MPF activity promoted the assembly through RhoA-mediated activation of MAPK, a decrease in MPF activity triggered contraction of the ring by activating RhoA. Public Library of Science 2010-09-13 /pmc/articles/PMC2938347/ /pubmed/20856880 http://dx.doi.org/10.1371/journal.pone.0012706 Text en Wu 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 Wu, Yan-Guang Zhou, Ping Lan, Guo-Cheng Gao, Da Li, Qing Wei, De-Li Wang, Hui-Li Tan, Jing-He MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes |
title | MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes |
title_full | MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes |
title_fullStr | MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes |
title_full_unstemmed | MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes |
title_short | MPF Governs the Assembly and Contraction of Actomyosin Rings by Activating RhoA and MAPK during Chemical-Induced Cytokinesis of Goat Oocytes |
title_sort | mpf governs the assembly and contraction of actomyosin rings by activating rhoa and mapk during chemical-induced cytokinesis of goat oocytes |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2938347/ https://www.ncbi.nlm.nih.gov/pubmed/20856880 http://dx.doi.org/10.1371/journal.pone.0012706 |
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