Possible involvement of mitogen- and stress-activated protein kinase 1, MSK1, in metaphase-II arrest through phosphorylation of EMI2 in mouse oocytes
| Autor: | Tadashi Baba, Yu Miyagaki, Yoshinori Kanemori |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
MAPK/ERK pathway
Oocyte Mouse MSK1 Molecular Sequence Data Xenopus EMI2 Ribosomal Protein S6 Kinases 90-kDa Cell Line Mice Animals Humans Amino Acid Sequence Phosphorylation Molecular Biology Metaphase DNA Primers Germinal vesicle biology Base Sequence Sequence Homology Amino Acid Kinase Reverse Transcriptase Polymerase Chain Reaction F-Box Proteins Cell Biology biology.organism_classification MAPK Cell biology Meiosis Mitogen-activated protein kinase Knockout mouse biology.protein Oocytes Developmental Biology Subcellular Fractions |
| Zdroj: | Developmental biology. 359(1) |
| ISSN: | 1095-564X |
| Popis: | Ovulated oocytes are arrested at the metaphase of second meiotic division. The metaphase-II arrest in Xenopus oocytes is regulated by RSKs located downstream of the Mos–MAPK pathway. In mice, other kinase(s) besides RSKs may be responsible for the metaphase-II arrest, because RSK1/RSK2/RSK3-triple knockout mice exhibit no obvious phenotype. Here, we show the subcellular localization and possible role of mitogen- and stress-activated kinase 1, MSK1 known as another downstream kinase of the Mos–MAPK pathway, in the mouse oocytes. Immunostaining analysis indicated that MSK1 is present in the germinal vesicle (GV) and cytoplasm of oocytes at the GV and metaphase-II stages, respectively. An active, phosphorylated form of MSK1 was predominantly localized to the metaphase-II spindle. The inhibition of the MSK1 activity failed to maintain the sister chromatid alignment within the metaphase-II plate. Importantly, MSK1 exhibited the ability to phosphorylate four Ser/Thr residues of meiotic cell-cycle regulator EMI2. The phosphorylation was required for up-regulation of the EMI2 activity in the oocytes. These results suggest that mouse MSK1 may play a key role in the metaphase-II arrest through phosphorylation of EMI2. |
| Databáze: | OpenAIRE |
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