Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology

Nat Struct Mol Biol. 2005 Sep;12(9):772-8. doi: 10.1038/nsmb979. Epub 2005 Aug 21.

Abstract

The binding of eukaryotic translation elongation factor 1A (eEF1A) to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression. Using the yeast Saccharomyces cerevisiae, we have established an in vivo assay that directly identifies specific regions and residues of eEF1A responsible for actin interactions and bundling. Using a unique genetic screen, we isolated a series of eEF1A mutants with reduced actin bundling activity. These mutations alter actin cytoskeleton organization but not translation, indicating that these are separate functions of eEF1A. This demonstrates for the first time a direct consequence of eEF1A on cytoskeletal organization in vivo and the physiological significance of this interaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism*
  • Asparagine / genetics
  • Asparagine / metabolism
  • Cell Proliferation
  • Cytoskeleton / metabolism*
  • Gene Expression Regulation, Fungal
  • Models, Molecular
  • Mutation / genetics
  • Peptide Elongation Factor 1 / chemistry
  • Peptide Elongation Factor 1 / genetics
  • Peptide Elongation Factor 1 / metabolism*
  • Phenotype
  • Phenylalanine / genetics
  • Phenylalanine / metabolism
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / cytology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Actins
  • Peptide Elongation Factor 1
  • Saccharomyces cerevisiae Proteins
  • TEF1 protein, S cerevisiae
  • Phenylalanine
  • Asparagine