Journal
DEVELOPMENTAL BIOLOGY
Volume 320, Issue 2, Pages 402-413Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ydbio.2008.05.548
Keywords
calcium; mammalian eggs; ERK; inositol 1,4,5-trisphosphate receptor; phosphorylation; polo
Categories
Funding
- NIH [HD051872, DK49194, DE 016289]
- National Science Foundation [BBS-8714235]
- FWO [G.0604.07, G.0210.03]
- K.U. Leuven [G.O.A. 2004/07]
- JSPS for Young Scientists
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To initiate embryo development, the sperm induces in the egg release of intracellular calcium ([Ca2+](i)). During oocyte maturation, the inositol 1,4,5-trisphosphate receptor (IP(3)R1), the channel implicated, undergoes modifications that enhance its function. We found that IP(3)R1 becomes phosphorylated during maturation at an MPM-2 epitope and that this persists until the fertilization-associated [Ca2+](i) responses cease. We also reported that maturation without ERK activity diminishes IP(3)R1 MPM-2 reactivity and [Ca2+](i) responses. Here, we show that IP(3)R1 is a novel target for Polo-like kinase1 (Plk1), a conserved M-phase kinase, which phosphorylates it at an MPM-2 epitope. Plk1 and IP(3)R1 interact in an M-phase preferential manner, and they exhibit close co-localization in the spindle/spindle poles area. This co-localization is reduced in the absence of ERK activity, as the ERK pathway regulates spindle organization and IP(3)R1 cortical re-distribution. We propose that IP(3)R1 phosphorylation by Plk1, and possibly by other M-phase kinases, underlies the delivery of spatially and temporally regulated [Ca2+](i) signals during meiosis/mitosis and cytokinesis. (C) 2008 Elsevier Inc. All rights reserved.
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