Requirement of yeast fimbrin for actin organization and morphogenesis in vivo

Nature. 1991 Dec 5;354(6352):404-8. doi: 10.1038/354404a0.


The SAC6 gene was found by suppression of a yeast actin mutation. Its protein product, Sac6p (previously referred to as ABP67), was independently isolated by actin-filament affinity chromatography and colocalizes with actin in vivo. Thus Sac6p binds to actin in vitro, and functionally associates with actin structures involved in the development and maintenance of cell polarity in vivo. We report here that Sac6p is an actin-filament bundling protein 43% identical in amino-acid sequence to the vertebrate bundling protein fimbrin. This yeast fimbrin homologue contains two putative actin-binding regions homologous to domains of dystrophin, beta-spectrin, filamin, actin-gelation protein and alpha-actinin. Mutants lacking Sac6p do not form normal actin structures and are defective in morphogenesis. These findings demonstrate an in vivo role for the well-documented biochemical interaction between fimbrin and actin.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actin Cytoskeleton / ultrastructure*
  • Actins / physiology*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Chickens
  • Genes, Fungal*
  • Humans
  • Macromolecular Substances
  • Membrane Glycoproteins / physiology*
  • Microfilament Proteins / physiology*
  • Microscopy, Electron
  • Molecular Sequence Data
  • Protein Conformation
  • Saccharomyces cerevisiae / physiology
  • Saccharomyces cerevisiae / ultrastructure
  • Sequence Alignment


  • Actins
  • Macromolecular Substances
  • Membrane Glycoproteins
  • Microfilament Proteins
  • plastin

Associated data

  • GENBANK/S67628
  • GENBANK/S68227
  • GENBANK/X57452
  • GENBANK/X57453
  • GENBANK/X57454
  • GENBANK/X57455
  • GENBANK/X62895
  • GENBANK/X62896
  • GENBANK/X62897
  • GENBANK/X63469