The cytoskeletal protein zyxin—A universal regulator of cell adhesion and gene expression

Research paper by L. V. Ermolina, N. Yu. Martynova, A. G. Zaraisky

Indexed on: 02 Feb '10Published on: 02 Feb '10Published in: Russian Journal of Bioorganic Chemistry


The attachment of a cell to the extracellular matrix or the surface of another cells affects not only the cell motility, but also gene expression. In view of this, an important problem is to establish the molecular mechanisms of signal transduction from the receptors of cell adhesion to the nucleus, in particular, to identify and investigate the protein transducers of these signals. One of these transducers, the LIM domain protein zyxin, is predominantly localized at the sites of cell adhesion, where it participates in the assembly of actin filaments. Owing to its location near the inner surface of the membrane, zyxin can interact with the transmembrane receptors of some signaling cascades and affect the signal transduction from the extracellular ligands of these receptors. Furthermore, under certain conditions, zyxin moves from the sites of cell contacts to the nucleus, where it directly participates in the regulation of gene expression. Of particular interest is the function of zyxin as a possible coordinator of gene expression and morphogenetic movements in embryogenesis. The published data discussed in the present review indicate the important role of zyxin in transmitting information from the regions of cell contacts to the genetic apparatus of the cell.