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Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins.

Zyxin contains a proline-rich N-terminal domain that is similar to the C-terminal domain in the ActA protein of the bacteria, Listeria monocytogenes. We screened the entire amino acid sequence of human zyxin for Mena-interacting peptides and found that, as with ActA, proline-rich sequences were the sole zyxin sequences capable of binding to Ena/vasodilator-stimulated phosphoprotein (VASP) family members in vitro. From this information, we tested zyxin mutants in which the proline-rich sequences were altered. The reduction in Mena/VASP binding was confirmed by peptide tests, immunoprecipitation, and ectopic expression of zyxin variants at the surface of mitochondria. By transfection assays we showed that zyxin interaction with Mena/VASP in vivo enhances the production of actin-rich structures at the apical surface of cells. Microinjection into cells of peptides corresponding to the first proline-rich sequence of zyxin caused the loss of Mena/VASP from focal contacts. Furthermore, these peptides reduced the degree of spreading of cells replated after trypsinization. We conclude that zyxin and proteins that harbor similar proline-rich repeats contribute to the positioning of Mena/VASP proteins. The positioning of Ena/VASP family members appears to be important when the actin cytoskeleton is reorganized, such as during spreading.

Pubmed ID: 10801818


  • Drees B
  • Friederich E
  • Fradelizi J
  • Louvard D
  • Beckerle MC
  • Golsteyn RM


The Journal of biological chemistry

Publication Data

July 21, 2000

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • Glycoproteins
  • Humans
  • Listeria monocytogenes
  • Metalloproteins
  • Microfilament Proteins
  • Molecular Sequence Data
  • Mutation
  • Phosphoproteins
  • Proline
  • Protein Binding
  • Zyxin