The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.

Many meiotic systems in female animals include a lengthy arrest in G2 that separates the end of pachytene from nuclear envelope breakdown (NEB). However, the mechanisms by which a meiotic cell can arrest for long periods of time (decades in human females) have remained a mystery. The Drosophila Matr...

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Autores principales:	Youbin Xiang, Satomi Takeo, Laurence Florens, Stacie E Hughes, Li-Jun Huo, William D Gilliland, Selene K Swanson, Kathy Teeter, Joel W Schwartz, Michael P Washburn, Sue L Jaspersen, R Scott Hawley
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2007
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/72c7a1a0309a4c889f589f837e437108
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spelling	oai:doaj.org-article:72c7a1a0309a4c889f589f837e4371082021-11-25T05:33:33ZThe inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.1544-91731545-788510.1371/journal.pbio.0050323https://doaj.org/article/72c7a1a0309a4c889f589f837e4371082007-12-01T00:00:00Zhttps://doi.org/10.1371/journal.pbio.0050323https://doaj.org/toc/1544-9173https://doaj.org/toc/1545-7885Many meiotic systems in female animals include a lengthy arrest in G2 that separates the end of pachytene from nuclear envelope breakdown (NEB). However, the mechanisms by which a meiotic cell can arrest for long periods of time (decades in human females) have remained a mystery. The Drosophila Matrimony (Mtrm) protein is expressed from the end of pachytene until the completion of meiosis I. Loss-of-function mtrm mutants result in precocious NEB. Coimmunoprecipitation experiments reveal that Mtrm physically interacts with Polo kinase (Polo) in vivo, and multidimensional protein identification technology mass spectrometry analysis reveals that Mtrm binds to Polo with an approximate stoichiometry of 1:1. Mutation of a Polo-Box Domain (PBD) binding site in Mtrm ablates the function of Mtrm and the physical interaction of Mtrm with Polo. The meiotic defects observed in mtrm/+ heterozygotes are fully suppressed by reducing the dose of polo+, demonstrating that Mtrm acts as an inhibitor of Polo. Mtrm acts as a negative regulator of Polo during the later stages of G2 arrest. Indeed, both the repression of Polo expression until stage 11 and the inactivation of newly synthesized Polo by Mtrm until stage 13 play critical roles in maintaining and properly terminating G2 arrest. Our data suggest a model in which the eventual activation of Cdc25 by an excess of Polo at stage 13 triggers NEB and entry into prometaphase.Youbin XiangSatomi TakeoLaurence FlorensStacie E HughesLi-Jun HuoWilliam D GillilandSelene K SwansonKathy TeeterJoel W SchwartzMichael P WashburnSue L JaspersenR Scott HawleyPublic Library of Science (PLoS)articleBiology (General)QH301-705.5ENPLoS Biology, Vol 5, Iss 12, p e323 (2007)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Youbin Xiang Satomi Takeo Laurence Florens Stacie E Hughes Li-Jun Huo William D Gilliland Selene K Swanson Kathy Teeter Joel W Schwartz Michael P Washburn Sue L Jaspersen R Scott Hawley The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.
description	Many meiotic systems in female animals include a lengthy arrest in G2 that separates the end of pachytene from nuclear envelope breakdown (NEB). However, the mechanisms by which a meiotic cell can arrest for long periods of time (decades in human females) have remained a mystery. The Drosophila Matrimony (Mtrm) protein is expressed from the end of pachytene until the completion of meiosis I. Loss-of-function mtrm mutants result in precocious NEB. Coimmunoprecipitation experiments reveal that Mtrm physically interacts with Polo kinase (Polo) in vivo, and multidimensional protein identification technology mass spectrometry analysis reveals that Mtrm binds to Polo with an approximate stoichiometry of 1:1. Mutation of a Polo-Box Domain (PBD) binding site in Mtrm ablates the function of Mtrm and the physical interaction of Mtrm with Polo. The meiotic defects observed in mtrm/+ heterozygotes are fully suppressed by reducing the dose of polo+, demonstrating that Mtrm acts as an inhibitor of Polo. Mtrm acts as a negative regulator of Polo during the later stages of G2 arrest. Indeed, both the repression of Polo expression until stage 11 and the inactivation of newly synthesized Polo by Mtrm until stage 13 play critical roles in maintaining and properly terminating G2 arrest. Our data suggest a model in which the eventual activation of Cdc25 by an excess of Polo at stage 13 triggers NEB and entry into prometaphase.
format	article
author	Youbin Xiang Satomi Takeo Laurence Florens Stacie E Hughes Li-Jun Huo William D Gilliland Selene K Swanson Kathy Teeter Joel W Schwartz Michael P Washburn Sue L Jaspersen R Scott Hawley
author_facet	Youbin Xiang Satomi Takeo Laurence Florens Stacie E Hughes Li-Jun Huo William D Gilliland Selene K Swanson Kathy Teeter Joel W Schwartz Michael P Washburn Sue L Jaspersen R Scott Hawley
author_sort	Youbin Xiang
title	The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.
title_short	The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.
title_full	The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.
title_fullStr	The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.
title_full_unstemmed	The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.
title_sort	inhibition of polo kinase by matrimony maintains g2 arrest in the meiotic cell cycle.
publisher	Public Library of Science (PLoS)
publishDate	2007
url	https://doaj.org/article/72c7a1a0309a4c889f589f837e437108
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The inhibition of polo kinase by matrimony maintains G2 arrest in the meiotic cell cycle.

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