Dmoesin Controls Actin-Based Cell Shape and Polarity During Drosophila Melanogaster Oogenesis

Nat Cell Biol. 2002 Oct;4(10):782-9. doi: 10.1038/ncb856.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actin Cytoskeleton / genetics
  • Actin Cytoskeleton / metabolism*
  • Animals
  • Blood Proteins / genetics
  • Blood Proteins / metabolism
  • Cell Polarity / genetics*
  • Cell Size / genetics
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism
  • Drosophila melanogaster / cytology
  • Drosophila melanogaster / embryology*
  • Drosophila melanogaster / metabolism
  • Female
  • Gene Expression Regulation, Developmental / genetics
  • Male
  • Membrane Proteins / deficiency*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Mutation / genetics
  • Oocytes / cytology
  • Oocytes / growth & development*
  • Oocytes / metabolism
  • Oogenesis / genetics*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism
  • Phylogeny
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Sequence Homology, Amino Acid
  • Threonine / genetics
  • Threonine / metabolism

Substances

  • Blood Proteins
  • Cytoskeletal Proteins
  • Drosophila Proteins
  • Membrane Proteins
  • Phosphoproteins
  • Recombinant Fusion Proteins
  • ezrin
  • moesin, Drosophila
  • osk protein, Drosophila
  • radixin
  • Threonine

Associated data

  • GENBANK/T29262
  • RefSeq/NP_002435
  • RefSeq/NP_002897
  • RefSeq/NP_003370
  • RefSeq/NP_033536
  • RefSeq/NP_110490
  • SWISSPROT/P26041
  • SWISSPROT/P26042
  • SWISSPROT/P31976
  • SWISSPROT/P46150