Biology:Zyxin

From HandWiki
Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Zyxin is a protein that in humans is encoded by the ZYX gene.[1][2][3]

Function

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.[3]

Interactions

Zyxin has been shown to interact with:

References

  1. "A zyxin-related protein whose synthesis is reduced in virally transformed fibroblasts". Eur J Biochem 241 (2): 657–63. January 1997. doi:10.1111/j.1432-1033.1996.00657.x. PMID 8917469. 
  2. "Molecular characterization of human zyxin". J Biol Chem 271 (49): 31470–8. January 1997. doi:10.1074/jbc.271.49.31470. PMID 8940160. 
  3. 3.0 3.1 "Entrez Gene: ZYX zyxin". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7791. 
  4. "An alpha-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment". J. Biol. Chem. 274 (19): 13410–8. May 1999. doi:10.1074/jbc.274.19.13410. PMID 10224105. 
  5. "Analysis of the alpha-actinin/zyxin interaction". J. Biol. Chem. 276 (36): 33328–35. September 2001. doi:10.1074/jbc.M100789200. PMID 11423549. 
  6. "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase". J. Biol. Chem. 278 (24): 21685–92. June 2003. doi:10.1074/jbc.M301447200. PMID 12672821. 
  7. 7.0 7.1 "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins". J. Biol. Chem. 275 (29): 22503–11. July 2000. doi:10.1074/jbc.M001698200. PMID 10801818. 
  8. "Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1". J. Biol. Chem. 279 (19): 20401–10. May 2004. doi:10.1074/jbc.M310304200. PMID 15004028. 
  9. "Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts/LATS1 tumor suppressor". J. Cell Biol. 149 (5): 1073–86. May 2000. doi:10.1083/jcb.149.5.1073. PMID 10831611. 
  10. "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. October 2000. doi:10.1074/jbc.M005066200. PMID 10882740. 

Further reading

External links