| The SUMO pathway functions in mouse oocyte maturation. | |
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MedLine Citation:
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PMID: 20543581 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sumoylation is an important post-translational modification in which SUMO (small ubiquitin-related modifier) proteins are bonded covalently to their substrates. Studies on the roles of sumoylation in cell cycle regulation have been emerging in both mitosis from yeast to mammals and meiosis in budding yeast, but the functions of sumoylation in mammalian meiosis, especially in oocyte meiotic maturation are not well known. Here, we examined the localization and expression of SUMO-1 and SUMO-2/3, the two basic proteins in the sumoylation pathway and investigated their roles through over-expression of Senp2 during mouse oocyte maturation. Immunofluorescent staining revealed differential patterns of SUMO-1 and SUMO-2/3 localization: SUMO-1 was localized to the spindle poles in prometaphase I, MI and MII stages, around the separating homologues in anaphase I and telophase I stages of first meiosis, while SUMO-2/3 was mainly concentrated near centromeres during mouse oocyte maturation. Immunoblot analysis uncovered the different expression profiles of SUMO-1 and SUMO-2/3 modified proteins during mouse oocyte maturation. Over-expression of Senp2, a SUMO-specific isopeptidase, caused changes of SUMO-modified proteins and led to defects in MII spindle organization in mature eggs. These results suggest that the SUMO pathway may play an indispensable role during mouse oocyte meiotic maturation. |
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Authors:
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Zhen-Bo Wang; Xiang-Hong Ou; Jing-Shan Tong; Sen Li; Liang Wei; Ying-Chun Ouyang; Yi Hou; Heide Schatten; Qing-Yuan Sun |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Cell cycle (Georgetown, Tex.) Volume: 9 ISSN: 1551-4005 ISO Abbreviation: Cell Cycle Publication Date: 2010 Jul |
Date Detail:
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Created Date: 2011-04-18 Completed Date: 2011-06-15 Revised Date: 2012-09-19 |
Medline Journal Info:
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Nlm Unique ID: 101137841 Medline TA: Cell Cycle Country: United States |
Other Details:
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Languages: eng Pagination: 2640-6 Citation Subset: IM |
Copyright Information:
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© 2010 Landes Bioscience |
Affiliation:
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State Key Laboratory of Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, China. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Differentiation* Female Gene Expression Profiling Meiosis Mice Mitotic Spindle Apparatus / metabolism Multienzyme Complexes / metabolism Oocytes / cytology*, metabolism* Protein Transport Signal Transduction* Small Ubiquitin-Related Modifier Proteins / metabolism* Subcellular Fractions / metabolism Sumoylation Time Factors |
| Chemical | |
Reg. No./Substance:
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0/Multienzyme Complexes; 0/Senp2 protein, mouse; 0/Small Ubiquitin-Related Modifier Proteins |
| Comments/Corrections | |
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