Regulation of inositol 1,4,5-trisphosphate receptor type 1 function during oocyte maturation by MPM-2 phosphorylation

被引:28
|
作者
Vanderheyden, Veerle [2 ]
Wakai, Takuya
Bultynck, Geert [2 ]
De Smedt, Humbert [2 ]
Parys, Jan B. [2 ]
Fissore, Rafael A. [1 ]
机构
[1] Univ Massachusetts, Dept Vet & Anim Sci, Paige Labs, Amherst, MA 01003 USA
[2] Katholieke Univ Leuven, Dept Mol & Cell Biol, Lab Mol & Cellular Signalling, B-3000 Louvain, Belgium
关键词
Calcium; Mammalian eggs; IP3R; Plk1; MPM-2; phosphorylation; Oocyte maturation; POLO-LIKE KINASE; MAMMALIAN EGG ACTIVATION; IN-VITRO MATURATION; MEIOTIC MATURATION; MOUSE OOCYTES; ENDOPLASMIC-RETICULUM; LIGAND-BINDING; CELL-CYCLE; TRISPHOSPHATE RECEPTOR; INTRACELLULAR CALCIUM;
D O I
10.1016/j.ceca.2009.04.004
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Egg activation and further embryo development require a sperm-induced intracellular Ca2+ signal at the time of fertilization. Prior to fertilization, the egg's Ca2+ machinery is therefore optimized. To this end, during oocyte maturation, the sensitivity, i.e. the Ca2+ releasing ability, of the inositol 1,4,5-trisphosphate receptor type 1 (IP(3)R1), which is responsible for most of this Ca2+ release, markedly increases. In this study, the recently discovered specific Polo-like kinase (Plk) inhibitor BI2536 was used to investigate the role of Plk1 in this process. BI2536 inactivates Plk1 in oocytes at the early stages of maturation and significantly decreases IP(3)R1 phosphorylation at an MPM-2 epitope at this stage. Moreover, this decrease in Plk1-dependent MPM-2 phosphorylation significantly lowers IP(3)R1 sensitivity. Finally, using in vitro phosphorylation techniques we identified T-2656 as a major Plk1 site on IP(3)R1. We therefore propose that the initial increase in IP(3)R1 sensitivity during oocyte maturation is underpinned by IP(3)R1 phosphorylation at an MPM-2 epitope(s). (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:56 / 64
页数:9
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