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The SUMO Pathway Functions in Mouse Oocyte Maturation

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Journal Cell Cycle
Specialty Cell Biology
Date 2010 Jun 15
PMID 20543581
Citations 26
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Abstract

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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References
1.
Dawlaty M, Malureanu L, Jeganathan K, Kao E, Sustmann C, Tahk S . Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha. Cell. 2008; 133(1):103-15. PMC: 2693193. DOI: 10.1016/j.cell.2008.01.045. View

2.
Pichler A, Gast A, Seeler J, Dejean A, Melchior F . The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell. 2002; 108(1):109-20. DOI: 10.1016/s0092-8674(01)00633-x. View

3.
Cheng C, Lo Y, Liang S, Ti S, Lin F, Yeh C . SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae. Genes Dev. 2006; 20(15):2067-81. PMC: 1536058. DOI: 10.1101/gad.1430406. View

4.
Sun S, Wei L, Li M, Lin S, Xu B, Liang X . Perturbation of survivin expression affects chromosome alignment and spindle checkpoint in mouse oocyte meiotic maturation. Cell Cycle. 2009; 8(20):3365-72. DOI: 10.4161/cc.8.20.9855. View

5.
Takahashi Y, Yong-Gonzalez V, Kikuchi Y, Strunnikov A . SIZ1/SIZ2 control of chromosome transmission fidelity is mediated by the sumoylation of topoisomerase II. Genetics. 2005; 172(2):783-94. PMC: 1456244. DOI: 10.1534/genetics.105.047167. View