ZYX

Focal adhesions are actin-rich structures that enable cells to adhere to the extracellular matrix and at which protein complexes involved in signal transduction assemble. Zyxin is a zinc-binding phosphoprotein that concentrates at focal adhesions and along the actin cytoskeleton. Zyxin has an N-terminal proline-rich domain and three LIM domains in its C-terminal half. The proline-rich domain may interact with SH3 domains of proteins involved in signal transduction pathways while the LIM domains are likely involved in protein-protein binding. Zyxin may function as a messenger in the signal transduction pathway that mediates adhesion-stimulated changes in gene expression and may modulate the cytoskeletal organization of actin bundles. Alternative splicing results in multiple transcript variants that encode the same isoform. [provided by RefSeq, Jul 2008]

Zyxin

Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity).

Cell-cell signalingManual Assertion Based On ExperimentTAS:ProtInc
Cell-matrix adhesion1 PublicationIC:UniProtKB
Cellular response to interferon-gammaIEA:Ensembl
Integrin-mediated signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Regulation of inflammatory responseIEA:Ensembl
Signal transductionManual Assertion Based On ExperimentIBA:GO_Central
Stress fiber assemblyManual Assertion Based On ExperimentIMP:UniProtKB
Transforming growth factor beta receptor signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB

Cytoplasm
Cytoplasm, cytoskeleton
Nucleus
Cell junction, focal adhesion
Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1.