title: Wispy, the Drosophila homolog of GLD-2, is required during oogenesis and egg activation.
abstract: Egg activation is the process that modifies mature, arrested oocytes so that embryo development can proceed. One key aspect of egg activation is the cytoplasmic polyadenylation of certain maternal mRNAs to permit or enhance their translation. wispy (wisp) maternal-effect mutations in Drosophila block development during the egg-to-embryo transition. We show here that the wisp gene encodes a member of the GLD-2 family of cytoplasmic poly(A) polymerases (PAPs). The WISP protein is required for poly(A) tail elongation of bicoid, Toll, and torso mRNAs upon egg activation. In Drosophila, WISP and Smaug (SMG) have previously been reported to be required to trigger the destabilization of maternal mRNAs during egg activation. SMG is the major regulator of this activity. We report here that SMG is still translated in activated eggs from wisp mutant mothers, indicating that WISP does not regulate mRNA stability by controlling the translation of smg mRNA. We have also analyzed in detail the very early developmental arrest associated with wisp mutations. Pronuclear migration does not occur in activated eggs laid by wisp mutant females. Finally, we find that WISP function is also needed during oogenesis to regulate the poly(A) tail length of dmos during oocyte maturation and to maintain a high level of active (phospho-) mitogen-activated protein kinases (MAPKs).
authors.affiliation: Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
authors.forename: Jun
authors.initials: J
authors.lastname: Cui
authors.forename: Katharine L
authors.initials: KL
authors.lastname: Sackton
authors.forename: Vanessa L
authors.initials: VL
authors.lastname: Horner
authors.forename: Kritika E
authors.initials: KE
authors.lastname: Kumar
authors.forename: Mariana F
authors.initials: MF
authors.lastname: Wolfner
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D029721:Drosophila Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000166:cytology* / Q000196:embryology / Q000201:enzymology*; D004625:Embryo, Nonmammalian / Q000378:metabolism; D004789:Enzyme Activation; D005260:Female; D008297:Male; D008540:Meiosis; D020928:Mitogen-Activated Protein Kinases / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation / Q000235:genetics; D009865:Oocytes / Q000201:enzymology*; D009866:Oogenesis; D011061:Poly A / Q000378:metabolism; D011062:Polynucleotide Adenylyltransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D014176:Protein Biosynthesis; D016601:RNA-Binding Proteins / Q000096:biosynthesis / Q000378:metabolism; D012097:Repressor Proteins / Q000096:biosynthesis; D017386:Sequence Homology, Amino Acid
chemical_list: C113767:BicC protein, Drosophila; D029721:Drosophila Proteins; D016601:RNA-Binding Proteins; D012097:Repressor Proteins; C402587:smg protein, Drosophila; D011061:Poly A; D020928:Mitogen-Activated Protein Kinases; D011062:Polynucleotide Adenylyltransferase