Regulation of inositol 1,4,5-trisphosphate receptor type 1 function during oocyte maturation by MPM-2 phosphorylation |
| |
| Authors: | Veerle Vanderheyden Takuya Wakai Geert Bultynck Humbert De Smedt Jan B. Parys Rafael A. Fissore |
| |
| Affiliation: | 1. Laboratory of Molecular and Cellular Signalling, Department of Molecular Cell Biology, K.U. Leuven, Campus Gasthuisberg, O&N1 Bus 802, B-3000 Leuven, Belgium;2. Department of Veterinary and Animal Sciences, University of Massachusetts, Amherst, MA 01003, USA;1. Department of Oral Pharmacology, School of Dentistry, Brain Korea 21 Plus Project, Chonbuk National University, Jeonju, Republic of Korea;2. Samsung Advanced Institute of Technology, Well Aging Research Center, Suwon, Republic of Korea;3. College of Natural Sciences, Kyungpook National University, Daegu, Republic of Korea;4. Natural Medicine Research Institute, Department of Pharmacy, College of Pharmacy, Mokpo National University, Jeonnam 534-729, Republic of Korea;5. Department of Animal Science and Technology, Sunchon National University, Suncheon, Republic of Korea;1. Département de Physique, Université Chouaïb Doukkali, El Jadida, Morocco;2. Lycée technique Louis Aragon, Héricourt, Franche-Comté, France;1. Department of Animal Sciences, Chungbuk National University, Cheongju, South Korea;2. Brain Korea 21 Center for Bio-Resource Development, Cheongju, South Korea;1. Department of Developmental Biology and Morphology of Invertebrates, Institute of Zoology, Jagiellonian University, Gronostajowa 9, 30-387 Kraków, Poland;2. Department of Zoology, Faculty of Biology and Environmental Protection, University of Silesia, Bankowa 9, 40-007 Katowice, Poland |
| |
| Abstract: | ![]()
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 (IP3R1), 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 IP3R1 phosphorylation at an MPM-2 epitope at this stage. Moreover, this decrease in Plk1-dependent MPM-2 phosphorylation significantly lowers IP3R1 sensitivity. Finally, using in vitro phosphorylation techniques we identified T2656 as a major Plk1 site on IP3R1. We therefore propose that the initial increase in IP3R1 sensitivity during oocyte maturation is underpinned by IP3R1 phosphorylation at an MPM-2 epitope(s). |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
