Calcineurin and its regulation by Sra/RCAN is required for completion of meiosis in Drosophila

Ca 2+ signaling pathways play important roles to complete meiosis from metaphase II arrest in vertebrate oocytes. However, less is known about the molecular mechanism of completion of meiosis in Drosophila females. Here, we provide direct evidence that calcineurin, a Ca 2+/calmodulin (CaM)-dependent...

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Bibliographic Details
Published in:Developmental biology 2010-08, Vol.344 (2), p.957-967
Main Authors: Takeo, Satomi, Hawley, R. Scott, Aigaki, Toshiro
Format: Article
Language:English
Subjects:
Anaphase
Animals
Calcineurin
Calcineurin - genetics
Calcineurin - metabolism
Chromosomes - metabolism
Drosophila
Drosophila - genetics
Drosophila - metabolism
Female
Female meiosis
Fertilization - genetics
Meiosis
Metaphase
Oocytes - metabolism
Oocytes - physiology
Phosphoric Monoester Hydrolases - genetics
Phosphoric Monoester Hydrolases - metabolism
Phosphorylation
RCANs
Signal Transduction - genetics
Signal Transduction - physiology
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Summary:Ca 2+ signaling pathways play important roles to complete meiosis from metaphase II arrest in vertebrate oocytes. However, less is known about the molecular mechanism of completion of meiosis in Drosophila females. Here, we provide direct evidence that calcineurin, a Ca 2+/calmodulin (CaM)-dependent phosphatase, is essential for meiotic progression beyond metaphase I in Drosophila oocytes. Oocytes from germline clones lacking CanB2, a calcineurin regulatory subunit B, failed to complete meiosis after egg activation, and laid eggs exhibited a meiotic arrested anaphase I chromosome configuration. Genetic analyses suggest that calcineurin activity is regulated by Sarah (Sra), a family member of regulators of calcineurin (RCANs), through a Sra phosphorylation-dependent mechanism. Our results support a view in which the phosphorylation of Sra not only acts to relieve the inhibitory effects of Sra, but also acts to activate calcineurin, thus explaining the role of RCAN proteins as positive regulators of calcineurin.
ISSN:0012-1606
1095-564X
DOI:10.1016/j.ydbio.2010.06.011