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• W1999232417 abstract "The Drosophila nuclear lamina protein YA is essential for the transition from female meiosis to embryo mitosis. Its localization and, hence, function is under developmental and cell cycle controls. YA protein is hyperphosphorylated and cytoplasmic in ovaries. Upon egg activation, YA is partially dephosphorylated and acquires the ability to enter nuclei. Its function is first detected at this time. To investigate the cytoplasmic retention machinery that keeps YA from entering nuclei, we used affinity chromatography and blot overlay assays to identify cytoplasmic proteins that associate with YA. Drosophila P0/AP3, a ribosomal protein that is also an apurinic/apyrimidinic endonuclease, binds to YA in ovary and embryo cytoplasms. P0 and YA bind specifically and directly in vitro and are present in a 20S complex in the cytoplasmic extracts. YA protein can be phosphorylated by MAPK, but not by p34Cdc2 kinase, in vitro. This phosphorylation increases YA's binding to P0. We propose that the P0-containing 20S cytoplasmic complex retains hyperphosphorylated ovarian YA in the cytoplasm. In response to egg activation, YA is partially dephosphorylated and its binding to the 20S complex is reduced. Hence, some YA dissociates from the complex and enters nuclei. Consistent with this model, decreasing P0 levels partially suppress a hypomorphic Ya mutant allele." @default.
• W1999232417 created "2016-06-24" @default.
• W1999232417 creator A5061747980 @default.
• W1999232417 creator A5073566367 @default.
• W1999232417 creator A5077640505 @default.
• W1999232417 date "2002-04-01" @default.
• W1999232417 modified "2023-10-16" @default.
• W1999232417 title "Interaction of the Essential Drosophila Nuclear Protein YA with P0/AP3 in the Cytoplasm and in Vitro: Implications for Developmental Regulation of YA's Subcellular Location" @default.
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• W1999232417 doi "https://doi.org/10.1006/dbio.2002.0601" @default.
• W1999232417 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11944949" @default.
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