A WD40 repeat protein regulates fungal cell differentiation and can be replaced functionally by the mammalian homologue striatin

Eukaryot Cell. 2004 Feb;3(1):232-40. doi: 10.1128/EC.3.1.232-240.2004.

Abstract

Fruiting body development in fungi is a complex cellular differentiation process that is controlled by more than 100 developmental genes. Mutants of the filamentous fungus Sordaria macrospora showing defects in fruiting body formation are pertinent sources for the identification of components of this multicellular differentiation process. Here we show that the sterile mutant pro11 carries a defect in the pro11 gene encoding a multimodular WD40 repeat protein. Complementation analysis indicates that the wild-type gene or C-terminally truncated versions of the wild-type protein are able to restore the fertile phenotype in mutant pro11. PRO11 shows significant homology to several vertebrate WD40 proteins, such as striatin and zinedin, which seem to be involved in Ca2+-dependent signaling in cells of the central nervous system and are supposed to function as scaffolding proteins linking signaling and eukaryotic endocytosis. Cloning of a mouse cDNA encoding striatin allowed functional substitution of the wild-type protein with restoration of fertility in mutant pro11. Our data strongly suggest that an evolutionarily conserved cellular process controlling eukaryotic cell differentiation may regulate fruiting body formation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ascomycota / cytology*
  • Ascomycota / metabolism*
  • Ascomycota / physiology
  • Blotting, Western
  • Calcium / metabolism
  • Calmodulin-Binding Proteins / metabolism
  • Calmodulin-Binding Proteins / physiology*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / physiology*
  • Cell Differentiation
  • Cloning, Molecular
  • Cosmids / metabolism
  • DNA / metabolism
  • DNA, Complementary / metabolism
  • Databases as Topic
  • Drosophila melanogaster
  • Fungal Proteins / physiology*
  • Genetic Complementation Test
  • Humans
  • Membrane Proteins / metabolism
  • Membrane Proteins / physiology*
  • Mice
  • Microscopy
  • Microscopy, Interference
  • Models, Genetic
  • Molecular Sequence Data
  • Mutation
  • Nerve Tissue Proteins / metabolism
  • Nerve Tissue Proteins / physiology*
  • Plasmids / metabolism
  • Polymerase Chain Reaction
  • Protein Structure, Tertiary
  • Rats
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Subcellular Fractions / metabolism

Substances

  • Calmodulin-Binding Proteins
  • Carrier Proteins
  • DNA, Complementary
  • Fungal Proteins
  • Membrane Proteins
  • Nerve Tissue Proteins
  • STRN protein, human
  • Strn protein, mouse
  • Strn protein, rat
  • DNA
  • Calcium