title: Calcineurin and its regulation by Sra/RCAN is required for completion of meiosis in Drosophila.
abstract: 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.
authors.affiliation: Stowers Institute for Medical Research, Kansas City, MO 64110, USA. sta@stowers.org
authors.forename: Satomi
authors.initials: S
authors.lastname: Takeo
authors.forename: R Scott
authors.initials: RS
authors.lastname: Hawley
authors.forename: Toshiro
authors.initials: T
authors.lastname: Aigaki
mesh_terms: D000705:Anaphase; D000818:Animals; D019703:Calcineurin / Q000235:genetics / Q000378:metabolism*; D002875:Chromosomes / Q000378:metabolism; D004330:Drosophila / Q000235:genetics* / Q000378:metabolism*; D005260:Female; D005306:Fertilization / Q000235:genetics; D008540:Meiosis; D008677:Metaphase; D009865:Oocytes / Q000378:metabolism / Q000502:physiology; D010744:Phosphoric Monoester Hydrolases / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D015398:Signal Transduction / Q000235:genetics / Q000502:physiology
chemical_list: D019703:Calcineurin; D010744:Phosphoric Monoester Hydrolases