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Dmoesin controls actin-based cell shape and polarity during Drosophila melanogaster oogenesis.
- Source :
-
Nature cell biology [Nat Cell Biol] 2002 Oct; Vol. 4 (10), pp. 782-9. - Publication Year :
- 2002
-
Abstract
- Ezrin, Radixin and Moesin (ERM) proteins are thought to constitute a bridge between the actin cytoskeleton and the plasma membrane (PM). Here we report a genetic analysis of Dmoesin, the sole member of the ERM family in Drosophila. We show that Dmoesin is required during oogenesis for anchoring microfilaments to the oocyte cortex. Alteration of the actin cytoskeleton resulting from Dmoesin mutations impairs the localization of maternal determinants, thus disrupting antero-posterior polarity. This study also demonstrates the requirement of Dmoesin for the specific organization of cortical microfilaments in nurse cells and, consequently, mutations in Dmoesin produce severe defects in cell shape.
- Subjects :
- Actin Cytoskeleton genetics
Animals
Blood Proteins genetics
Blood Proteins metabolism
Cell Size genetics
Cytoskeletal Proteins genetics
Cytoskeletal Proteins metabolism
Drosophila Proteins genetics
Drosophila Proteins metabolism
Drosophila melanogaster cytology
Drosophila melanogaster metabolism
Female
Gene Expression Regulation, Developmental genetics
Male
Membrane Proteins genetics
Membrane Proteins metabolism
Molecular Sequence Data
Mutation genetics
Oocytes cytology
Oocytes metabolism
Phosphoproteins genetics
Phosphoproteins metabolism
Phylogeny
Protein Structure, Tertiary
Recombinant Fusion Proteins
Sequence Homology, Amino Acid
Threonine genetics
Threonine metabolism
Actin Cytoskeleton metabolism
Cell Polarity genetics
Drosophila melanogaster embryology
Membrane Proteins deficiency
Oocytes growth & development
Oogenesis genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1465-7392
- Volume :
- 4
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Nature cell biology
- Publication Type :
- Academic Journal
- Accession number :
- 12360288
- Full Text :
- https://doi.org/10.1038/ncb856