Zyxin: zinc fingers at sites of cell adhesion

Bioessays. 1997 Nov;19(11):949-57. doi: 10.1002/bies.950191104.


Zyxin is a low abundance phosphoprotein that is localized at sites of cell-substratum adhesion in fibroblasts. Zyxin displays the architectural features of an intracellular signal transducer. The protein exhibits an extensive proline-rich domain, a nuclear export signal and three copies of the LIM motif, a double zinc-finger domain found in many proteins that play central roles in regulation of cell differentiation. Zyxin interacts with alpha-actinin, members of the cysteine-rich protein (CRP) family, proteins that display Src homology 3 (SH3) domains and Ena/VASP family members. Zyxin and its partners have been implicated in the spatial control of actin filament assembly as well as in pathways important for cell differentiation. Based on its repertoire of binding partners and its behavior, zyxin may serve as a scaffold for the assembly of multimeric protein machines that function in the nucleus and at sites of cell adhesion.

Publication types

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

MeSH terms

  • Actinin / metabolism
  • Amino Acid Sequence
  • Cell Adhesion / physiology*
  • Extracellular Matrix / chemistry
  • Extracellular Matrix / metabolism
  • Metalloproteins / chemistry
  • Metalloproteins / metabolism*
  • Models, Biological
  • Molecular Sequence Data
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism
  • Protein Binding
  • Signal Transduction / physiology
  • Zinc Fingers / physiology*


  • Metalloproteins
  • Phosphoproteins
  • Actinin