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PMID: 18430932 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Wispy, the Drosophila homolog of GLD-2, is required during oogenesis and egg activation.

Genetics ·Vol. 178 ·No. 4 ·2008-04-00 ·Pages 2017-29

Cui J, Sackton KL, Horner VL, Kumar KE, Wolfner MF

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).

MeSH Terms
Amino Acid Sequence Animals Drosophila Proteins/biosynthesis,chemistry,genetics,metabolism Drosophila melanogaster/cytology,embryology,enzymology Embryo, Nonmammalian/metabolism Enzyme Activation Female Male Meiosis Mitogen-Activated Protein Kinases/metabolism Molecular Sequence Data Mutation/genetics Oocytes/enzymology Oogenesis Poly A/metabolism Polynucleotide Adenylyltransferase/chemistry,genetics,metabolism Protein Binding Protein Biosynthesis RNA-Binding Proteins/biosynthesis,metabolism Repressor Proteins/biosynthesis Sequence Homology, Amino Acid
Chemicals
BicC protein, Drosophila Drosophila Proteins RNA-Binding Proteins Repressor Proteins smg protein, Drosophila Poly A Mitogen-Activated Protein Kinases Polynucleotide Adenylyltransferase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Cui Jun
Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.
Sackton Katharine L
Horner Vanessa L
Kumar Kritika E
Wolfner Mariana F
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Article Info
Journal
Genetics
Abbr.
Genetics
ISSN
0016-6731
Published
2008-04-00
Pages
2017-29
Language
English
Region
United States
NLM ID
0374636
PMCID
PMC2323793
Subset
IM
Grants
NIGMS NIH HHS · R01 GM044659 · United States
NIGMS NIH HHS · GM44659 · United States
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