Zyxin (ZYX) ELISA Kit for Human

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. Interacts with HPV type 6 protein E6. Does not interact significantly with E6 proteins from HPV types 11, 16, or 18. Interacts, via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP. Interacts with the first LIM domain of TES. Interacts with NEBL (isoform 2). Belongs to the zyxin/ajuba family.

Protein type: Cell adhesion; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 7q32

Cellular Component: focal adhesion; cell-cell adherens junction; integral to plasma membrane; cytoplasm; stress fiber; plasma membrane; nucleus

Molecular Function: protein binding; zinc ion binding

Biological Process: integrin-mediated signaling pathway; cell-cell signaling; viral reproduction; cell-matrix adhesion; transforming growth factor beta receptor signaling pathway; regulation of inflammatory response; stress fiber formation; cell adhesion; signal transduction