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Gene Review

ZYX  -  zyxin

Gallus gallus

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High impact information on ZYX

  • We have recently purified and characterized a low abundance adhesion plaque protein called zyxin (Crawford, A. W., and M. C. Beckerle. 1991. J. Biol. Chem. 266:5847-5853; Crawford, A. W., J. W. Michelsen, and M. C. Beckerle. 1992. J. Cell Biol. 116:1381-1393) [1].
  • By double-label indirect immunofluorescence, we found that zyxin and cCRP are extensively colocalized in chicken embryo fibroblasts, consistent with the idea that they interact in vivo [1].
  • LIM domains have been proposed to coordinate metal ions and we have demonstrated by atomic absorption spectroscopy that purified zyxin binds zinc, a result consistent with the idea that zyxin has zinc fingers [1].
  • The demonstration that two cytoskeletal proteins, zyxin and cCRP, share a sequence motif with proteins important for transcriptional regulation raises the possibility that zyxin and cCRP are components of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression [1].
  • Moreover, all three CRP isoforms are capable of interacting with the cytoskeletal proteins alpha-actinin and zyxin [2].

Biological context of ZYX


Anatomical context of ZYX

  • We show that the cTES protein localised at focal adhesions, actin stress fibres, and sites of cell-cell contact, and GST-cTES can pull-down zyxin and actin [4].
  • Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions [5].
  • Since the 82-kDa protein is found at both cell-substratum and cell-cell adherens junctions, we propose to call it zyxin, meaning a joining, to indicate that it is found at regions where extracellular ligands are structurally and functionally joined to the cytoskeleton [5].

Associations of ZYX with chemical compounds


Analytical, diagnostic and therapeutic context of ZYX


  1. Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton. Sadler, I., Crawford, A.W., Michelsen, J.W., Beckerle, M.C. J. Cell Biol. (1992) [Pubmed]
  2. Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression. Louis, H.A., Pino, J.D., Schmeichel, K.L., Pomiès, P., Beckerle, M.C. J. Biol. Chem. (1997) [Pubmed]
  3. LIM domains of cysteine-rich protein 1 (CRP1) are essential for its zyxin-binding function. Schmeichel, K.L., Beckerle, M.C. Biochem. J. (1998) [Pubmed]
  4. Characterisation of chicken TES and its role in cell spreading and motility. Griffith, E., Coutts, A.S., Black, D.M. Cell Motil. Cytoskeleton (2004) [Pubmed]
  5. Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions. Crawford, A.W., Beckerle, M.C. J. Biol. Chem. (1991) [Pubmed]
  6. Chick sensory neuronal growth cones distinguish fibronectin from laminin by making substratum contacts that resemble focal contacts. Gomez, T.M., Roche, F.K., Letourneau, P.C. J. Neurobiol. (1996) [Pubmed]
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